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R M Macnab

Publications and source records attributed to R M Macnab.

At least 19 recordsLinked to original sources
PubMed1992

Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body.

The direction of rotation of the bacterial flagellum is determined by the flagellar switch. We have localized FliG, one of the switch proteins of Salmonella typhimurium, to the cytoplasmic face of the M ring of the flagellar basal body. This localization was made possible by the discovery of two spontaneous mutants in which the fliF (M ring) and fliG (switch) genes were fused in-frame. In the first mutant, a deletion of 7 base pairs at the 3' end of fliF resulted in an essentially full-length fusion protein. In the second mutant, a larger deletion resulted in a fusion in which 56 amino acids from the carboxyl terminus of FliF and 94 amino acids from the amino terminus of FliG were lost. Both strains were motile and underwent switching; the first strain had a clockwise bias, and the second strain had a counterclockwise bias. Gel electrophoresis and immunoblotting of isolated hook-basal-body complexes verified that they contained the fusion proteins. Electron microscopy revealed additional mass at the cytoplasmic face of the M ring, which could be decorated with anti-FliG antibody. We conclude that the natural location for FliG is at the cytoplasmic face of the M ring and that the stoichiometric ratio between FliF and FliG in wild-type cells is probably 1:1.

Amino Acid Sequence↗
PubMed1992

Subdivision of flagellar region III of the Escherichia coli and Salmonella typhimurium chromosomes and identification of two additional flagellar genes.

The many genes involved in flagellar structure and function in Escherichia coli and Salmonella typhimurium are located in three major clusters on the chromosome: flagellar regions I, II and III. We have found that region III does not consist of a contiguous set of flagellar genes, as was thought, but that in E. coli there is almost 7 kb of DNA between the filament cap gene, fliD, and the next known flagellar gene, fliE; a similar situation occurs in S. typhimurium. Most of this DNA is unrelated to flagellar function, since a mutant in which 5.4 kb of it had been deleted remained fully motile and chemotactic as judged by swarming on semi-solid agar. We have therefore subdivided flagellar region III into two regions, IIIa and IIIb. The known genes in region IIIa are fliABCD, all of which are involved in filament structure and assembly, while region IIIb contains genes fliEFGHIJKLMNOPQR, all of which are related to formation of the hook (basal-body)-complex or to even earlier assembly events. We have found that fliD, the last known gene in region IIIa, is immediately followed by two additional genes, both necessary for flagellation, which we have designated fliS and fliT. They encode small proteins with deduced molecular masses of about 15 kDa and 14 kDa, respectively. The functions of FliS and FliT remain to be determined, but they do not appear to be members of the axial family of structural proteins to which FliD belongs.

Amino Acid Sequence↗
PubMed1992

Escherichia coli produces a cytoplasmic alpha-amylase, AmyA.

In the gap between two closely linked flagellar gene clusters on the Escherichia coli and Salmonella typhimurium chromosomes (at about 42 to 43 min on the E. coli map), we found an open reading frame whose sequence suggested that it encoded an alpha-amylase; the deduced amino acid sequences in the two species were 87% identical. The strongest similarities to other alpha-amylases were to the excreted liquefying alpha-amylases of bacilli, with > 40% amino acid identity; the N-terminal sequence of the mature bacillar protein (after signal peptide cleavage) aligned with the N-terminal sequence of the E. coli or S. typhimurium protein (without assuming signal peptide cleavage). Minicell experiments identified the product of the E. coli gene as a 56-kDa protein, in agreement with the size predicted from the sequence. The protein was retained by spheroplasts rather than being released with the periplasmic fraction; cells transformed with plasmids containing the gene did not digest extracellular starch unless they were lysed; and the protein, when overproduced, was found in the soluble fraction. We conclude that the protein is cytoplasmic, as predicted by its sequence. The purified protein rapidly digested amylose, starch, amylopectin, and maltodextrins of size G6 or larger; it also digested glycogen, but much more slowly. It was specific for the alpha-anomeric linkage, being unable to digest cellulose. The principal products of starch digestion included maltotriose and maltotetraose as well as maltose, verifying that the protein was an alpha-amylase rather than a beta-amylase. The newly discovered gene has been named amyA. The natural physiological role of the AmyA protein is not yet evident.

Amino Acid Sequence↗
PubMed1992

Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium.

Defects in the chemotaxis proteins CheY and CheZ of Salmonella typhimurium can be suppressed by mutations in the flagellar switch, such that swarming of a pseudorevertant on semisolid plates is significantly better than that of its parent. cheY suppressors contribute to a clockwise switch bias, and cheZ suppressors contribute to a counterclockwise bias. Among the three known switch genes, fliM contributes most examples of such suppressor mutations. We have investigated the changes in FliM that are responsible for suppression, as well as the changes in CheY or CheZ that are being compensated for. Ten independently isolated parental cheY mutations represented nine distinct mutations, one an amino acid duplication and the rest missense mutations. Several of the altered amino acids lie on one face of the three-dimensional structure of CheY (A. M. Stock, J. M. Mottonen, J. B. Stock, and C. E. Schutt, Nature (London) 337:745-749, 1989; K. Volz and P. Matsumura, J. Biol. Chem. 266:15511-15519, 1991); this face may constitute the binding site for the switch. All 10 cheZ mutations were distinct, with several of them resulting in premature termination. cheY and cheZ suppressors in FliM occurred in clusters, which in general did not overlap. A few cheZ suppressors and one cheY suppressor involved changes near the N terminus of FliM, but neither cheY nor cheZ suppressors involved changes near the C terminus. Among the strongest cheY suppressors were changes from Arg to a neutral amino acid or from Val to Glu, suggesting that electrostatic interactions may play an important role in switching. A given cheY or cheZ mutation could be suppressed by many different fliM mutations; conversely, a given fliM mutation was often encountered as a suppressor of more than one cheY or cheZ mutation. The data suggest that an important factor in suppression is a balancing of the shift in switch bias introduced by alteration of CheY or CheZ with an appropriate opposing shift introduced by alteration of FliM. For strains with a severe parental mutation, such as the cheZ null mutations, adjustment of switch bias is essentially the only factor in suppression, since the attractant L-aspartate caused at most a slight further enhancement of the swarming rate over that occurring in the absence of a chemotactic stimulus. We discuss a model for switching in which there are distinct interactions for the counterclockwise and clockwise states, with suppression occurring by impairment of one of the states and hence by relative enhancement of the other state. FliM can also undergo amino acid changes that result in a paralyzed (Mot-) phenotype; these changes were confined to a very few residues in the protein.

Amino Acid Sequence↗
PubMed1992

Characterization of the fliE genes of Escherichia coli and Salmonella typhimurium and identification of the FliE protein as a component of the flagellar hook-basal body complex.

Within flagellar region III of Escherichia coli and Salmonella typhimurium, the genomic organization has been largely established. An exception is fliE, a gene whose exact location and product function are not well understood. We cloned the fliE gene, obtained its DNA sequence, and identified its product.fliE was found to be a monocistronic transcriptional unit, adjacent to and divergent from the large fliF operon. It is several kilobases distant from the nearest flagellar operon in the other direction, the fliD operon, and constitutes the first operon within the newly defined region IIIb, which contains the genes fliE through fliR.fliE encodes a small, moderately hydrophilic protein with a deduced molecular mass of 11,114 Da (E. coli) or 11,065 Da (S. typhimurium). We identified a protein within the isolated hook-basal body complex as the fliE gene product on the basis of its size and comparison of its N-terminal amino acid sequence with that deduced from the gene sequence. From gel electrophoresis and autoradiography of 35S-labeled S. typhimurium hook-basal body complexes (C.J. Jones, R.M. Macnab, H. Okino, and S.-I. Aizawa, J. Mol. Biol. 212:377-387, 1990) and the deduced number of sulfur-containing residues in FliE, we estimated the stoichiometry of the protein in the hook-basal body complex to be about nine subunits. FliE does not undergo cleavage of a signal peptide, nor does it show any sequence similarity to the axial components like the rod or hook proteins, which are believed to be exported by the flagellum-specific export pathway. On the basis of this and other evidence, we suggest that FliE may be in the vicinity of the MS ring, perhaps acting as an adaptor protein between the ring and rod substructures.

Amino Acid Sequence↗
PubMed1991

Genetic analysis of the bacterial flagellum.

Escherichia coli and Salmonella typhimurium invest considerable resources in making flagella, motor organelles that function much like the propellers on a ship. Both classical and molecular genetic studies have begun to reveal how flagellar genes are regulated and how their products build and operate these remarkable devices.

Cell Movement↗
PubMed1991

Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits.

Many flagellar proteins are exported by a flagellum-specific export pathway. In an initial attempt to characterize the apparatus responsible for the process, we designed a simple assay to screen for mutants with export defects. Temperature-sensitive flagellar mutants of Salmonella typhimurium were grown at the permissive temperature (30 degrees C), shifted to the restrictive temperature (42 degrees C), and inspected in a light microscope. With the exception of switch mutants, they were fully motile. Next, cells grown at the permissive temperature had their flagellar filaments removed by shearing before the cells were shifted to the restrictive temperature. Most mutants were able to regrow filaments. However, flhA, fliH, fliI, and fliN mutants showed no or greatly reduced regrowth, suggesting that the corresponding gene products are involved in the process of flagellum-specific export. We describe here the sequences of fliH, fliI, and the adjacent gene, fliJ; they encode proteins with deduced molecular masses of 25,782, 49,208, and 17,302 Da, respectively. The deduced sequence of FliI shows significant similarity to the catalytic beta subunit of the bacterial F0F1 ATPase and to the catalytic subunits of vacuolar and archaebacterial ATPases; except for limited similarity in the motifs that constitute the nucleotide-binding or catalytic site, it appears unrelated to the E1E2 class of ATPases, to other proteins that mediate protein export, or to a variety of other ATP-utilizing enzymes. We hypothesize that FliI is either the catalytic subunit of a protein translocase for flagellum-specific export or a proton translocase involved in local circuits at the flagellum.

Amino Acid Sequence↗
PubMed1990

Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum.

Within the bacterial flagellum the basal-body rod, the hook, the hook-associated proteins (HAPs), and the helical filament constitute an axial substructure whose elements share structural features and a common export pathway. We present here the amino acid sequences of the hook protein and the three HAPs of Salmonella typhimurium, as deduced from the DNA sequences of their structural genes (flgE, flgK, flgL and fliD, respectively). We compared these sequences with each other and with those for the filament protein (flagellin) and four rod proteins, which have been described previously (Joys, 1985; Homma et al., 1990; Smith & Selander, 1990). Hook protein most strongly resembled the distal rod protein (FlgG) and the proximal HAP (HAP1), which are thought to be attached to the proximal and distal ends of the hook, respectively; the similarities were most pronounced near the N and C termini. Hook protein and flagellin, which occupy virtually identical helical lattices, did not resemble each other strongly but showed some limited similarities near their termini. HAP3 and HAP2, which form the proximal and distal boundaries of the filament, showed few similarities to flagellin, each other, or the other axial proteins. With the exceptions of the N-terminal region of HAP2, and the C-terminal region of flagellin, proline residues were absent from the terminal regions of the axial proteins. Moreover, with the exception of the N-terminal region of HAP2, the terminal regions contained hydrophobic residues at intervals of seven residues. Together, these observations suggest that the axial proteins may have amphipathic alpha-helical structure at their N and C termini. In the case of the filament and the hook, the terminal regions are believed to be responsible for the quaternary interactions between subunits. We suggest that this is likely to be true of the other axial structures as well, and specifically that interaction between N-terminal and C-terminal alpha-helices may be important in the formation of the axial structures of the flagellum. Although consensus sequences were noted among some of the proteins, such as the rod, hook and HAP1, no consensus extended to the entire set of axial proteins. Thus the basis for recognition of a protein for export by the flagellum-specific pathway remains to be identified.

Amino Acid Sequence↗
PubMed1990

Steady-state measurements of Escherichia coli sodium and proton potentials at alkaline pH support the hypothesis of electrogenic antiport.

31P and 23Na NMR spectroscopy was applied to the measurement of proton and sodium potentials in endogenously respiring Escherichia coli cells over an external pH (pHex) range from mildly acidic (6.4) to fairly alkaline (8.4). Stable maintenance of alkaline pHex in the face of metabolic acidification was achieved by use of a perfusion system. In the acidic to neutral pHex range, the sodium chemical potential followed the proton chemical potential quite closely, although always exceeding it slightly, as has been reported previously (Castle, A. M., Macnab, R. M., and Shulman, R. G. (1986) J. Biol. Chem. 261, 7797-7806). Above pHex 7.4, the sodium potential changed abruptly from a decreasing to an increasing function of pHex, whereas the proton potential continued to decrease. As a consequence, the apparent stoichiometry (i.e. the ratio between the sodium and proton electrochemical potentials) took on progressively higher values, increasing from approximately 1.1 at pH 7.4 to approximately 1.3 at pH 7.8. Thereafter, the sodium chemical potential started to decrease again; however, since the decrease was less steep than that of the proton potential, the apparent stoichiometry continued to increase. At the highest pHex examined (8.4), it had reached a value of approximately 1.4. These results strongly support the hypothesis of an electroneutral (1:1) H+/Na+ antiporter operating virtually alone under acidic to neutral conditions and then being supplemented to an ever increasing degree by an electrogenic (for example, 2:1) antiporter under more alkaline conditions.

Biological Transport↗
PubMed1990

Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium.

The stoichiometries of components within the flagellar hook-(basal-body) complex of Salmonella typhimurium have been determined. The hook protein (FlgE), the most abundant protein in the complex, is present at approximately 130 subunits. Hook-associated protein 1 (FlgK) is present at approximately 12 subunits. The distal rod protein (FlgG) is present at approximately 26 subunits, while the proximal rod proteins (FlgB, FlgC and FlgF) are present at only approximately six subunits each. The stoichiometries of the proximal rod proteins and hook-associated protein 1 are, within experimental error, consistent with values of 5 or 6, and 11, respectively. Such values would correspond to either one or two turns of a helical structure with a basic helix of approximately 5.5 subunits per turn, which is the geometry of both the hook and the filament and, one supposes, the rod and hook-associated proteins. These stoichiometries may derive from rules for the heterologous interactions that occur when a helical structure consists of successive segments constructed from different proteins; the stoichiometries within the hook and the distal portion of the rod must, however, be set by different mechanisms. The stoichiometries for the ring proteins are approximately 26 subunits each for the M-ring protein (FliF), the P-ring protein (FlgI), and the L-ring protein (FlgH); the protein responsible for the S-ring feature is not known. The rings presumably have rotational rather than helical symmetry, in which case the stoichiometries would be directly constrained by the intersubunit bonding angle. The ring stoichiometries are discussed in light of other information concerning flagellar structure and function.

Amino Acid Sequence↗
PubMed1990

Pausing, switching and speed fluctuation of the bacterial flagellar motor and their relation to motility and chemotaxis.

Wild-type Escherichia coli and Salmonella typhimurium cells, tethered to glass by their flagella, rotate with brief intermittent pauses, the prevalence of which is decreased by attractants and increased by repellents. By attaching latex beads to filaments of a S. typhimurium mutant having straight rather than helical flagella, it was established that the flagella on free cells also pause intermittently. Pausing is therefore an intrinsic feature of the motor and not an artifact associated with tethering. In tethered cells of wild-type strains and non-chemotactic mutants defective in transducers, chemotaxis proteins, or the flagellar switch, both the classical response to chemotactic stimuli (change in direction of rotation from counterclockwise to clockwise or vice versa), and the pausing response to such stimuli, were linked together. No separate signal for pausing was found. In comparing different strains under different stimulation conditions, it was found that cells that never reversed seldom if ever paused, while cells that reversed frequently paused frequently. It is suggested that pausing is the result of futile switching events. A modified description of tumbling and chemotaxis is provided in which pausing, as well as reversal, has a role. Suppression of reversals and pauses by attractant stimuli commonly resulted in an increase in the speed of counterclockwise rotation; this may be because of suppression of pauses or reversals that are too brief to be detected. The clockwise rotation rate of unstimulated cells, which commonly was faster than their counterclockwise rate, was not further increased by repellent stimuli. The rotation rate of any given cell under any given condition was found to fluctuate on all time-scales measured. The study also revealed that some of the common repellents of E. coli and S. typhimurium slow down or stop the motor; these effects are not mediated by the chemotaxis machinery or intracellular pH.

Cell-Free System↗
PubMed1990

FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium.

The flagellar basal body of Salmonella typhimurium consists of four rings surrounding a rod. The rod, which is believed to transmit motor rotation to the filament, is not well characterized in terms of its structure and composition. FlgG is known to lie within the distal portion of the rod, in the region where it is surrounded by the L and P rings, just before the rod-hook junction. The FlgC and FlgF proteins are also known to be flagellar basal-body components; by comparison of deduced and experimental N-terminal amino acid sequences we show here that FlgB is a basal-body protein. The flgB, flgC, flgF and flgG gene sequences and the deduced protein sequences are presented. The four proteins are clearly related to each other in primary sequence, especially toward the N and C termini, supporting the hypothesis (based on examination of basal-body subfractions) that FlgB, FlgC and FlgF are, like FlgG, rod proteins. From this and other information we suggest that the rod is the cell-proximal part of a segmented axial structure of the flagellum, with FlgB, FlgC and FlgF located (in unknown order) in successive segments of the proximal rod, followed by FlgG located in the distal rod; the axial structure then continues with the hook, HAPs and filament. Although the rod is external to the cell membrane, none of the four rod proteins contains a consensus signal sequence for the primary export pathway; comparison with the experimentally determined N-terminal amino acid sequence indicates that FlgB has had its N-terminal methionine removed, while the other three are not processed at all. This demonstrates that these proteins are not exported by the primary cellular pathway, and suggests that they are exported by the same flagellum-specific pathway as the flagellar filament protein flagellin. The observed sequence similarities among the rod proteins, especially a six-residue consensus motif about 30 residues in from the N terminus, may constitute a recognition signal for this pathway or they may reflect higher-order structural similarities within the rod.

Amino Acid Sequence↗
PubMed1990

Repellent response functions of the Trg and Tap chemoreceptors of Escherichia coli.

The chemoreceptors responsible for the repellent response of Escherichia coli to phenol were investigated. In the absence of all four known methyl-accepting chemoreceptors (Tar, Tsr, Trg, and Tap), cells showed no response to phenol. However, when Trg, which mediates the attractant response to ribose and galactose, was introduced via a plasmid, the cells acquired a repellent response to phenol. About 1 mM phenol induced a clear repellent response; this response was suppressed by 1 mM ribose. Thus, Trg mediates the repellent response to phenol. Mutant Trg proteins with altered sensing for ribose and galactose showed a normal response to phenol, indicating that the interaction site for phenol differs from that for the ribose- and galactose-binding proteins. Tap, which mediates the attractant response to dipeptides, mediated a weaker repellent response to phenol. Tsr, which mediates the attractant response to serine, mediated an even weaker response to phenol. Trg and Tap were also found to function as intracellular pH sensors. Upon a pH decrease, Trg mediated an attractant response, whereas Tap mediated a repellent response. These results indicate that all the receptors in E. coli have dual functions, mediating both attractant and repellent responses.

Bacterial Proteins↗
PubMed1990

Flagellar assembly in Salmonella typhimurium: analysis with temperature-sensitive mutants.

The process of flagellar assembly in Salmonella typhimurium was investigated by using temperature-sensitive mutants. The mutants were grown at the restrictive temperature and then at the permissive temperature, with radiolabel supplied in the first phase of the experiment and not the second, or vice versa. Flagellar hook-basal body complexes were then purified and analyzed by gel electrophoresis and autoradiography. The extent to which a given protein was labeled in the two phases of the experiment provided information as to whether it preceded or followed the block caused by the mutant protein. We conclude the following concerning flagellar assembly. The M-ring protein (FliF) is stably incorporated in the earliest stage detected, along with two previously unknown proteins, with apparent molecular masses of 23 and 26 kilodaltons, respectively, and possibly one of the switch components, FliG. Independent of that event and all other events, the P-ring and L-ring proteins (FlgI and FlgH) are synthesized and exported to the periplasm and outer membrane by the primary cellular export pathway. Rod assembly occurs by export (via the flagellum-specific pathway) of subunits of four proteins, FlgB, FlgC, FlgF, and FlgG, and their incorporation, probably in that order, into the rod structure; this stage requires the flhA and fliI genes, perhaps because they encode part of the export apparatus. Once rod assembly is complete, the FlgI and FlgH proteins assemble around the rod to form the P and L rings. The rod structure, which is only metastable while it is being constructed, becomes stable upon P-ring addition. Export (via the flagellum-specific pathway) and assembly of hook protein, hook-associated proteins, and filament protein then occur successively. A number of flagellar proteins, whose genetic origin and structural role are not yet known, were identified on the basis of their dependence on the flagellar master operon for expression.

Bacterial Proteins↗
PubMed1990

Co-overproduction and localization of the Escherichia coli motility proteins motA and motB.

The motility genes motA and motB of Escherichia coli were placed under control of the Serratia marcescens trp promoter. After induction with beta-indoleacrylic acid, the levels of MotA and MotB rose over about a 3-h period, reaching plateau levels approximately 50-fold higher than wild-type levels. Both overproduced proteins inserted into the cytoplasmic membrane. Growth and motility were essentially normal, suggesting that although the motor is a proton-conducting device, MotA and MotB together do not constitute a major proton leak. Derivative plasmids which maintained an intact version of motB but had the motA coding region deleted in various ways were constructed. With these, the levels of MotB were much lower, reaching a peak within 30 min after induction and declining thereafter; pulse-chase measurements indicated that a contributing factor was MotB degradation. The low levels of MotB occurred even with an in-frame internal deletion of motA, whose translational initiation and termination sites were intact, suggesting that it is the MotA protein, rather than the process of MotA synthesis, that is important for MotB stability. Termination at the usual site of overlap with the start of motB (ATGA) was not an absolute requirement for MotB synthesis but did result in higher rates of synthesis than when translation of motA information terminated prematurely. Even in the total absence of MotA, the MotB that was synthesized was found exclusively in the cytoplasmic membrane fraction. In wild-type cells, MotA was estimated by immunoprecipitation to be in about fourfold excess over MotB; a previous estimate of 600 +/- 250 copies of MotA per cell then yielded an estimate of 150 +/- 70 copies of MotB per cell.

Bacterial Proteins↗
PubMed1989

Image reconstruction of the flagellar basal body of Salmonella typhimurium.

The basal body is thought to be a part of the rotary motor of the bacterial flagellum. It consists of a central rod coaxial with a set of four rings, which are associated with the cell envelope. We used single-particle averaging methods to analyze images of negatively stained basal bodies of Salmonella typhimurium. Several averages were computed, so that the reliability of features could be assessed. We carried out the same analysis on electron micrographs of isolated, negatively stained L-P rings. In order to interpret the averages in terms of a three-dimensional structure, we carried out image reconstruction on them. The resulting three-dimensional map corresponds to the cylindrically averaged structure of the basal body. To show that the reconstruction procedure is legitimate, we demonstrate it on model data. The results of the modelling show that features very near to the axis of the reconstruction are not reliable but that broader, off-axis features are represented faithfully. The L ring is L-shaped, with the long arm of the L parallel to the axis of the rod, and the short arm pointing away from the rod. The P ring, on the other hand, appears to be a ring or disk. The position of the L-P ring complex on the rod seems to vary somewhat, consistent with its putative role as a bushing. The cross-sectional shape of the S ring is that of a frustum rather than a disk. The M ring, which is oval in cross section, sits atop the S ring, making contact with it at an outer radius. The S ring appears to make contact with the rod, whereas the M ring does not. This situation, if true, is difficult to reconcile with the common notion that the S ring is stationary and the M ring rotates. It seems more likely that the S ring and rod rotate as a unit.

Flagella↗
PubMed1989

Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway.

Flagellin and several other external components of the bacterial flagellum are thought to be exported, not by the general N-terminal signal peptide-dependent pathway, but by a flagellum-specific pathway involving a central channel in the flagellum itself. We have constructed a variety of mutant alleles of the Escherichia coli flagellin gene. Mutant flagellins with large internal deletions or truncations of their C-terminal region could still be exported, even though they could not assemble into filament. The most extreme example was a fragment containing only the N-terminal 183 residues of the 497-residue wild-type flagellin. This result suggests that the N-terminal region of flagellin contains a signal that enables the protein to be recognized and exported by the flagellum-specific pathway.

Amino Acid Sequence↗