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PubMed2004

Preparation and characterization of monoclonal antibodies against S1 domain at N-terminal residues 249 to 667 of SARS-associated coronavirus S1 protein.

OBJECTIVE: To prepare and characterize monoclonal antibodies (mAbs) against S1 protein of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV). METHODS: 6-His-tagged recombinant fragment at N-terminal residues 249 to 667 of SARS-CoV S1 protein including S-protein receptor-binding domain was expressed in E.coli. The immunogenicity of this S1 domain was identified and used to immunize BALB/c mice for the production of hybridomas. The identification of the mAbs against this S1 domain was performed using indirect enzyme-linked immunosorbent assay (ELISA), indirect immunofluorescence assay (IFA) and Western blotting, respectively. RESULTS: Three hybridomas producing mAbs specific to the S1 domain was obtained, with a relative molecular mass of 48,500. None of the 3 mAbs were reactive with human coronaviruses 229E and OC43. Two of the mAbs were IgG2a isotype, and the other was IgG1. CONCLUSIONS: This is the first report of mAbs produced against S-protein receptor-binding domain of SARS-CoV. The 3 S1-specific mAbs may be useful for further study of the function of the S protein and for diagnosis of SARS-CoV infection.

Animals↗
PubMed2002

Ribosomal protein S1 induces a conformational change of tmRNA; more than one protein S1 per molecule of tmRNA.

tmRNA (10Sa RNA, ssrA) acts to rescue stalled bacterial ribosomes while encoding a peptide tag added trans-translationally to the nascent peptide, targeting it for proteolysis. Ribosomal protein S1 is required for tmRNA binding to isolated and poly U-programmed ribosomes. Mobility assays on native gels indicate that the binding curves of both recombinant and purified proteins S1 from E. coli is biphasic with apparent binding constants of approximately 90 and approximately 300 nM, respectively, suggesting that more than one protein interacts with tmRNA. Structural probing of native tmRNA in the presence and absence of the purified protein suggest that when S1 binds, tmRNA undergoes a significant conformational change. In the presence of the protein, nucleotides from tmRNA with enhanced (H2, H3, PK1, PK2, PK4, in and around the first triplet to be translated), or decreased (H5 and PK2), reactivity towards a probe specific for RNA single-strands are scattered throughout the molecule, with the exception of the tRNA-like domain that may be dispensable for the interaction. Converging experimental evidence suggests that ribosomal protein S1 binds to pseudoknot PK2. Previous structural studies of tmRNA in solution have revealed several discrepancies between the probing data and the phylogeny, and most of these are reconciled when analyzing tmRNA structure in complex with the protein(s). Ribosomal protein(s) S1 is proposed to set tmRNA in the mRNA mode, relieving strains that may develop when translating a looped mRNA.

Autoradiography↗
PubMed1995

ADP-ribosylation of alpha i3C20 by the S1 subunit and deletion peptides of S1 of pertussis toxin.

Recombinant S1 subunit of PT (rS1) and two carboxyl-terminal deletion peptides, C180 and C204, which comprise the amino-terminal 180 and 204 amino acids of S1, respectively, were analyzed for the ability to ADP-ribosylate alpha i3C20, a synthetic peptide composed of the 20 carboxyl-terminal amino acids of the alpha subunit of the heterotrimeric G protein Gi3. Under linear velocity conditions, C180 ADP-ribosylated alpha i3C20 at a 3-fold higher rate than either C204 or rS1. At variable NAD, rS1, C204, and C180 ADP-ribosylated alpha i3C20 with similar initial velocities which followed Michaelis-Menten kinetics. In contrast, at variable alpha i3C20, rS1, C204, and C180 ADP-ribosylated alpha i3C20 with different initial velocities. At variable alpha i3C20, C204- and rS1-catalyzed ADP-ribosylation followed Michaelis-Menten kinetics, while the velocity curve generated by C180 diverged from Michaelis-Menten kinetics. The rates of initial velocity of C180 did not fit the Lineweaver-Burk equation, but could be transformed into the Hill equation which yielded a Hill coefficient of 2. This predicted that C180 possessed cooperativity between the two substrate binding sites. Other experiments showed that C180 ADP-ribosylated alpha i3C20 at 60% of the rate for the ADP-ribosylation of Gt. These data showed that the entire catalytic mechanism for ADP-ribosylation resides within the first 180 amino acids of S1 and that the carboxyl-terminal 55 residues of S1 allow the ADP-ribosylation of alpha i3C20 to proceed via Michaelis-Menten kinetics. These data along with earlier studies (Krueger & Barbieri, 1993) were also consistent with the presence of two Gt protein binding sites within S1.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed2005

No evidence from FTIR difference spectroscopy that aspartate-170 of the D1 polypeptide ligates a manganese ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II.

On the basis of mutagenesis and X-ray crystallographic studies, Asp170 of the D1 polypeptide is widely believed to ligate the (Mn)4 cluster that is located at the catalytic site of water oxidation in photosystem II. Recent proposals for the mechanism of water oxidation postulate that D1-Asp170 ligates a Mn ion that undergoes oxidation during one or more of the S0 --> S1, S1 --> S2, and S2 --> S3 transitions. To test these hypotheses, we have compared the FTIR difference spectra of the individual S state transitions in wild-type* PSII particles from the cyanobacterium Synechocystis sp. PCC 6803 with those in D1-D170H mutant PSII particles. Remarkably, our data show that the D1-D170H mutation does not significantly alter the mid-frequency regions (1800-1000 cm(-1)) of any of the FTIR difference spectra. Therefore, we conclude that the oxidation of the (Mn)4 cluster does not alter the frequencies of the carboxylate stretching modes of D1-Asp170 during the S0 --> S1, S1 --> S2, or S2 --> S3 transitions. The simplest explanation for these data is that the Mn ion that is ligated by D1-Asp170 does not increase its charge or oxidation state during any of these S state transitions. These data have profound implications for the mechanism of water oxidation. Either (1) the oxidation of the Mn ion that is ligated by D1-Asp170 occurs only during the transitory S3 --> S4 transition and serves as the critical step in the ultimate formation of the O-O bond or (2) the oxidation increments and O2 formation chemistry that occur during the catalytic cycle involve only the remaining Mn3Ca portion of the Mn4Ca cluster. Our data also show that, if the increased positive charge on the (Mn)4 cluster that is produced during the S1 --> S2 transition is delocalized over the (Mn)4 cluster, it is not delocalized onto the Mn ion that is ligated by D1-Asp170.

Aspartic Acid↗
PubMed1997

Low-temperature interactions of NO with the S1 and S2 states of the water-oxidizing complex of photosystem II. A novel Mn-multiline EPR signal derived from the S1 state.

The spin-1/2-carrying NO molecule interacts with both the S1 and S2 states of the water oxidizing complex. The intermediates of the interaction can be resolved and trapped by NO treatment at subzero temperatures. At -30 degrees C and in the presence of approx. 500-700 microM NO, S1 loses the ability to yield by illumination an EPR active S2-state with an approximate half-time of 40-60 min. At longer incubation times (t1/2 = 4-5 h), an intense new multiline signal develops. The new signal has a hyperfine splitting similar to the S2 multiline [Dismukes, G. C., & Siderer, Y. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 274-278], but a modified shape with intense lines on the high field side. The NO modified S1 state can act as a low-temperature electron donor yielding an EPR silent state upon illumination at 200 K. NO interacts also with the S2 state of the water oxidizing complex rapidly at temperatures as low as -75 degrees C, to yield an EPR silent state. The rates of the latter interaction show analogies to the ammonia binding to the S2 state. It is possible, however, that NO, unlike ammonia, destabilizes the S2 state. On the basis of preliminary experiments with varying chloride concentrations in the range 0.1-50 mM, the S1 multiline state is attributed to binding of NO at a chloride sensitive site on the Mn cluster. The rapid interactions with the S2 state as well as the intermediate binding to the S1 state are less well understood at present, but they are tentatively assigned to the chloride-insensitive site of ammonia binding in the Mn cluster.

Cold Temperature↗
PubMed1998

Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus.

By combining site-directed mutagenesis with chemical modification, we have altered the S1 and S1' pocket specificity of subtilisin Bacillus lentus (SBL) through the incorporation of unnatural amino acid moieties, in the following manner: WT --> Cysmutant + H3CSO2SR --> Cys-SR, where R may be infinitely variable. A paradigm between extent of activity changes and surface exposure of the modified residue has emerged. Modification of M222C, a buried residue in the S1' pocket of SBL, caused dramatic changes in kcat/KM, of an up to 122-fold decrease, while modification of S166C, which is located at the bottom of the S1 pocket and is partially surface exposed, effected more modest activity changes. Introduction of a positive charge at S166C does not alter kcat/KM, whereas the introduction of a negative charge results in lowered activity, possibly due to electrostatic interference with oxyanion stabilization. Activity is virtually unaltered upon modification of S156C, which is located toward the bottom of the S1 pocket and surface exposed and whose side chain is solvated. An unexpected structure-activity relationship was revealed for S166C-SR enzymes in that the pattern of activity changes observed with increasing steric size of R was not monotonic. Molecular modeling analysis was used to analyze this unprecedented structure-activity relationship and revealed that the position of the beta-carbon of Cys166 modulates binding of the P1 residue of the AAPF product inhibitor.

Amino Acid Substitution↗
PubMed2006

Minimum 5-year analysis of L5-S1 fusion using sacropelvic fixation (bilateral S1 and iliac screws) for spinal deformity.

STUDY DESIGN: Clinical radiographic and outcomes investigation. OBJECTIVE: To investigate clinical and radiographic outcomes for lumbosacral fusion (in patients with spinal deformity) using a combination of bilateral sacral and iliac screws with a minimum 5-year follow-up. SUMMARY OF BACKGROUND DATA: To our knowledge, long-term results (>5 years of follow-up) of bilateral S1 screw/bilateral iliac screw fixation have never been published or presented. MATERIALS AND METHODS: A total of 67 patients (from an initial consecutive cohort of 81) undergoing lumbosacral fusion with bilateral sacral and iliac screws with a minimum follow-up of 5 years (range 5-10 + 5, average 6 + 3) were analyzed for radiographic outcome and clinical course by an outcome questionnaire (administered at ultimate follow-up) analysis. Patients were divided into 2 groups: group 1, 34 patients with mostly high-grade spondylolisthesis; and group 2, 33 with adult scoliosis fused mostly from the thoracic spine to the sacrum. A true anteroposterior pelvis film was obtained in all patients to assess for sacroiliac joint arthritis, as were standard spine radiographs. Patients were administered Oswestry and directed buttock pain questionnaires at latest follow-up. RESULTS: There were no cases of sacral screw failure (i.e., screw loosening, partial screw pullout, or fracture of the sacral screw). There were 5 cases of nonunion at L5-S1. Of the 5 cases, 3 did not have anterior column support at L5-S1. Four of the 5 cases were revised, and, subsequently, 3 achieved union. Iliac screws were removed electively on 1 or both sides in 23 of the patients after 2 years postoperatively because of prominence. There were 7 cases of iliac screw breakage. Iliac screw halos were observed in 29 patients. No sacroiliac osteoarthritis was observed on the true anteroposterior pelvis films. At ultimate follow-up, average visual analog painscale (0-10) score to assess buttock pain was 2.4, and average Oswestry score was 20.1. CONCLUSIONS: For high-grade spondylolisthesis and long adult deformity fusions to the sacrum, a montage of bilateral S1 screws and iliac screws were effective in protecting the sacral screws from failure. Pseudarthrosis at L5-S1 was manifested by rod breakage at that level. We saw no evidence of a long-term effect of the iliac screws predisposing the sacroiliac joints to degeneration at follow-up ranging from 5 to 10 years.

Adolescent↗
PubMed1999

Limited (L4-S1, L5-S1) selective dorsal rhizotomy for reducing spasticity in cerebral palsy.

Selective posterior rhizotomy is effective for relieving spasticity associated with cerebral palsy. In current techniques dorsal roots from L1/L2 to S1/S2 are selectively divided. With transoperative electromyography (EMG) significant sensory loss has been prevented, but postoperative hypotonia following excessive reduction of the fusimotor drive is still of concern for surgeons and therapists. To decrease the volume of deafferentiated rootlets we proposed a limited selective posterior rhizotomy (LPSR) that limits the extent of the surgery to three (L4-S1) or two (L5-S1) dorsal roots. We present the results of two group of spastic children; group 1 (n = 59, 32 quadriplegic and 27 diplegic) who had a L4-S1 LPSR, and group 2 (n = 12) in whom L5 and S1 were selectively rhizotomized. Posture, passive movilization, range of joint movement, and muscle tone in hip flexors, adductors, leg flexors and plantar flexors were graded according to the method proposed by Sindou and Jeanmonod. In all groups these was a significant reduction of the mentioned parameters (Friedman test p < 0.001) at 6, 12 and 18 months after surgery. The preoperative and postoperative ability to ambulate was classified into five grades. In all groups there was a significant (chi 2 between p < 0.01 and p < 0.001) improvement in the quality of their gait. A third of the patients achieved some form of independent ambulation. Our results suggest that extensive selective deafferentation of the lower limbs is not an absolute requisite for reducing muscle tone or achieving functional improvement in spastic children.

Cerebral Palsy↗
PubMed2005

Using DNA shuffling to create novel infectious bronchitis virus S1 genes: implications for S1 gene recombination.

We employed the staggered extension process (StEP) to shuffle the S1 genes from four infectious bronchitis virus (IBV) strains representing four unique serotypes. Upon creating a shuffled S1 gene library, we randomly selected 25 clones and analyzed them by DNA sequencing. In total, eleven clones contained novel S1 gene recombinants. Based on sequence data, each recombinant was unique and contained a full-length open reading frame. The average number of crossovers per recombinant was 5 and the average number of point mutations was 1.3, leading mostly to non-synonymous amino acid changes. No recombinant contained sequences from all four parental genes and no recombinant contained any sequence from the distantly related Delaware 072 strain. Our data suggests that recombination between distantly related IBV strains within the S1 gene probably does not readily occur. This finding is extremely important in light of the common industry vaccination practice of mixing different live-attenuated IBV strains.

Animals↗
PubMed1997

Calponin inhibits actin-activated MgATPase of myosin subfragment 1 (S1) without displacing S1 from its binding site on actin.

Calponin is a smooth-muscle thin-filament protein implicated in the regulation of contraction. Its binding to actin is a prerequisite for inhibition of actin-activated myosin MgATPase. Investigating the molecular mechanism of this inhibition, it was found that titration of acto-myosin subfragment 1 with calponin in the presence of either ADP or ATP does not displace weakly or strongly bound myosin subfragment 1 (S1) from actin. S1.ADP, however, is able to release about two-thirds of the calponin from saturated (equimolar) complexes of actin-calponin. The remaining calponin is sufficient for almost full inhibition of acto-S1 MgATPase activity. Bunding of actin filaments by calponin takes place at a higher ratio calponin/actin (above 1:3) and, therefore, is not responsible for inhibition of the ATPase. Bundle formation is inhibited by S1.ADP. These results suggest the existence of two calponin-binding sites on actin; one, that is insensitive to S1, which is responsible for inhibition of the ATPase, the other, from which calponin is readily displaced by S1.

Actins↗
PubMed2003

The new strategy for allele identification of the genes coding for pertussis toxin subunit S1 (ptx S1) and pertactin (prn) in Bordetella pertussis.

Bordetella pertussis strains demonstrate polymorphism in toxin subunit S1 (PT S1) and pertactin (Prn), which belong to major protective antigens of the pathogen. Changes in the distribution of particular alleles of ptxS1 and prn genes in local B. pertussis populations have been proposed as possible factors influencing the vaccination effectiveness. We have developed a new methodology for the identification of the alleles, which eliminates the necessity of DNA sequencing. The approach is based on the evaluation of the number of sequence repeats and detection of specific nucleotides at polymorphic sites of the genes, and utilizes products of their full or partial PCR amplification. The approach is available for a laboratory with standard equipment. The total conformity of the strategy with the DNA sequencing-based approach was proved on the full set of reference strains and a group of Polish clinical isolates. The new methodology was used to investigate a collection of 120 Polish B. pertussis strains isolated from the 1960s to 2001. Similarly to findings from other countries and to earlier Polish data, the tendency to change the vaccine types of PT S1 and Prn by the antigenically different ones was observed.

Alleles↗
PubMed1998

X-ray absorption spectroscopy on layered photosystem II membrane particles suggests manganese-centered oxidation of the oxygen-evolving complex for the S0-S1, S1-S2, and S2-S3 transitions of the water oxidation cycle.

By application of microsecond light flashes the oxygen-evolving complex (OEC) was driven through its functional cycle, the S-state cycle. The S-state population distribution obtained by the application of n flashes (n = 0. 6) was determined by analysis of EPR spectra; Mn K-edge X-ray absorption spectra were collected. Taking into consideration the likely statistical error in the data and the variability stemming from the use of three different approaches for the determination of edge positions, we obtained an upshift of the edge position by 0.8-1.5, 0.5-0.9, and 0.6-1.3 eV for the S0-S1, S1-S2, and S2-S3 transitions, respectively, and a downshift by 2.3-3.1 eV for the S3-S0 transition. These results are highly suggestive of Mn oxidation state changes for all four S-state transitions. In the S0-state spectrum, a clearly resolved shoulder in the X-ray spectrum around 6555 eV points toward the presence of Mn(II). We propose that photosynthetic oxygen evolution involves cycling of the photosystem II manganese complex through four distinct oxidation states of this tetranuclear complex: Mn(II)-Mn(III)-Mn(IV)2 in the S0-state, Mn(III)2-Mn(IV)2 in the S1-state, Mn(III)1-Mn(IV)3 in the S2-state, and Mn(IV)4 in the S3-state.

Chloroplasts↗
PubMed1987

A combination of RNase H and S1 nuclease circumvents an artefact inherent to conventional S1 analysis of RNA splicing.

S1 nuclease mapping is commonly used to analyze transcription and processing of unlabelled RNAs. However, the S1 protocol that appears best suited to demonstrate splicing of a particular RNA (using an intronless probe that is 5' end-labelled in the downstream exon) is not diagnostic as expected. Rather, both intron-containing RNA and intronless RNA confer protection of probe across the splice juncture. To unambiguously demonstrate correctly spliced RNAs that begin at a specific initiation site, we present a procedure in which unspliced RNA molecules are first cleaved by RNase H following annealing to an intronic DNA fragment and the remaining RNA is then subjected to S1 analysis using an intronless probe present in vast excess. Only spliced, correctly initiated transcripts can protect the probe across the splice junction and up to residue +1. This RNase H/S1 method provides a broadly applicable technique with which to demonstrate splicing and initiation of a variety of transcripts, especially ones from transfected genes that can arise both from the normal and from activated cryptic initiation sites.

Endonucleases↗
PubMed1985

Surprising S1-resistant trimolecular hybrids: potential complication in interpretation of S1 mapping analyses.

Although the technique of S1 mapping is a powerful analytical tool for the analysis of RNA, we now report a surprising complication involving a trimolecular hybrid between two RNA species and a single DNA probe molecule which, if unrecognized, can lead to misleading interpretations. We document that such trimolecular hybrids can be efficiently formed under some hybridization conditions and that the probe DNA sequence at the junction of the two RNA molecules can be remarkably stable to digestion with S1. Trimolecular hybrids can arise in any instance whenever a distal region of an end-labeled DNA probe is homologous to a moderately abundant RNA in the sample to be analyzed. This situation presents a serious, potential complication for a variety of S1 analyses, particularly those in which DNA transfection has been utilized to reintroduce in vitro-engineered genes into cultured animal cells.

Acetyltransferases↗
PubMed2003

Activation of the RegB endoribonuclease by the S1 ribosomal protein is due to cooperation between the S1 four C-terminal modules in a substrate-dependant manner.

The RegB protein, encoded by the T4 bacteriophage genome, is a ribonuclease involved in the inactivation of the phage early messenger RNAs. Its in vitro activity is very low but can be enhanced up to 100-fold in the presence of the ribosomal protein S1. The latter is made of six repeats of a conserved module found in many other proteins of RNA metabolism. Considering the difference between its size (556 amino acids) and that of several RegB substrates (10 nucleotides), we wondered whether all six modules are necessary for RegB activation. We studied the influence of twelve S1 fragments on the cleavage efficiency of three short substrates. RegB activation requires the cooperation of different sets of modules depending on the substrates. Two RNAs are quite well cleaved in the presence of the fragment formed by the fourth and fifth modules, whereas the third requires the presence of the four C-terminal domains. However, NMR interaction experiments showed that, despite these differences, the interactions of the substrates with either the bi- or tetra-modules are similar, suggesting a common interaction surface. In the case of the tetra-module the interactions involve all four domains, raising the question of the spatial organization of this region.

Amino Acid Sequence↗
PubMed2003

Fracture of S1-2 after L4-S1 decompression and fusion. Case report and review of the literature.

The author describes a woman in whom an S1-2 fracture developed after L4-S1 decompression and fusion. Osteoporosis was not present, but the lesion failed to respond to conservative therapy, necessitating surgical extension of the spinal fusion. Although biomechanical complications of lumbosacral fusion are uncommon, pseudarthrosis, degenerative spondylolisthesis, and stress fractures have been reported. To date, only four cases of sacral stress fracture appear in the literature, all involving female patients and reportedly associated with osteoporosis. Unlike the present case, the fracture resolved satisfactorily in all cases with conservative treatment.

Adult↗
PubMed1977

[Substrate inhibition as a cause of oscillations in an open irreversible enzymic reaction S1 + S2 in the presence of E(R,T) leads to S1' + S2'. A mathematical model].

A mathematical model of an open irreversible reaction S1 + S2 (formula: see text) catalysed by an olygomeric enzyme E(R, T) has been analysed. It is assumed that the enzyme undergoes the concerted conformational transitions R in equilibrium T in conformity with the theory of Monod, Wyman and Changeux, and one of the substrates (S2) produces inhibition of the enzyme, thus shifting the equilibrium between the two enzyme forms in the direction of T formation. A simple graphical explanation is given to the hysteresis of the input characteristic approximately v ([S1]) (approximately v is the reaction rate at d[S2]/dt=O) which gives rise to self--oscillations. The hysteresis occurs both in the case of allosteric and isosteric substrate inhibition.

Allosteric Regulation↗