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PubMed1987

Changes in penicillin-binding proteins during the life cycle of Micromonospora.

The penicillin-binding proteins (PBPs) of Micromonospora were studied. Only one PBP (48,000 mol weight) was found in membranes isolated from primary mycelia, whereas three PBPs were observed in secondary mycelia and designated PBP 1 (89,000 mol weight), PBP2 (69,000) and PBP3 (48,000). Both the unique PBP produced by primary mycelia and PBP3 of secondary mycelia had the same affinity for penicillin which was higher than that of PBP2 and 3. The role of these proteins in the cell life cycle of Micromonospora is discussed.

Bacterial Proteins↗
PubMedDate not supplied

[Comparative study of the lipid composition of seven species of "Micromonospora"].

Analysis of the lipids of seven species of Micromonospora showed the constant presence of five phospholipids and three glycolipids. The phospholipids were identified as cardiolipids, phosphatidylethanolamine, phosphatidyl-inositol, mannosides of phosphatidyl-inositol, and possibly lysocardiolipids. The glycolipids were monoglucosyl-diglycerides, diglucosyl-diglycerides (with a small amount of galactosyl-glucosyl-diglycerides) and esters of fatty acids and trehalose. The simultaneous presence of glucosyl-diglycerides and trehalose esters might be specific of the genus Micromonospora. In the seven species studied, a large amount of the total fatty acids (obtained by direct saponification of the cells) consisted of iso and anteiso fatty acids. Three groups could be distinguished, having respectively iso-C15, iso-C16 and n-C17 fatty acids as the main members. A monounsaturated C17 acid has been identified as heptadec-9,10-enoic acid.

Chemical Phenomena↗
PubMed2005

Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms.

Mutants of the Micromonospora viridifaciens sialidase, Y370E and Y370F, are catalytically active retaining enzymes that operate by different mechanisms. Previous substitutions with smaller amino acids, including Y370D, yielded inverting sialidases. At least one water molecule can fit into the active-site cavity of this mutant and act as a nucleophile from the face opposite the leaving group (Biochemistry 2003, 42, 12 682). Thus, addition of a CH(2) unit (Asp versus Glu) changes the mechanism from inversion back to retention of configuration. Based on Brønsted beta(lg) values, it is proposed that the Y370E mutant reacts by a double-displacement mechanism (beta(lg) on k(cat)/K(m) -0.36+/-0.04) with Glu370 acting as the nucleophile. However, the Y370F mutant (beta(lg) on k(cat)/K(m) -0.79+/-0.12) reacts via a dissociative transition state. The crystal structure of the Y370F mutant complexed with 2-deoxy-2,3-dehydro-N-acetylneuraminic acid shows no significant active-site perturbation relative to the wild-type enzyme.

Amino Acid Substitution↗
PubMed1994

Characterization and expression of a P-450-like mycinamicin biosynthesis gene using a novel Micromonospora-Escherichia coli shuttle cosmid vector.

A 29 kb shuttle cosmid vector, pTYS507, was constructed from a cryptic Micromonospora griseorubida plasmid and the Escherichia coli cosmid pJB8. Subcloning of mycinamicin II biosynthesis genes in pTYS507 led to the identification of a DNA region that could complement a mutant of M. griseorubida that lacked both hydroxylase and epoxidase activities. Nucleotide sequence and mutational analysis suggested that a single P-450-like protein catalyzes both reactions.

Amino Acid Sequence↗
PubMed1984

Involvement of 16S ribosomal RNA in resistance of the aminoglycoside-producers Streptomyces tenjimariensis, Streptomyces tenebrarius and Micromonospora purpurea.

Resistance to aminoglycoside antibiotics in Micromonospora purpurea (the producer of gentamicin C complex), Streptomyces tenebrarius (the nebramycin producer) and Streptomyces tenjimariensis (which makes istamycin) occurs at the level of the ribosome. Reconstitution analysis has revealed, in each case, that 16S rRNA plays a critical role in determining such resistance.

Aminoglycosides↗
PubMed1985

Methylation of 16S ribosomal RNA and resistance to the aminoglycoside antibiotics gentamicin and kanamycin determined by DNA from the gentamicin-producer, Micromonospora purpurea.

When DNA fragments from Micromonospora purpurea (the producer of gentamicin) were cloned in Streptomyces lividans, a gentamicin-resistant strain was obtained in which the ribosomes were highly resistant both to gentamicin and to kanamycin. Reconstitution analysis revealed that such resistance resulted from some property of their 16S RNA. Extracts from the clone contained methylase activity which acted on 16S RNA within E. coli 30S ribosomal subunits and rendered them resistant to gentamicin and kanamycin.

DNA, Bacterial↗
PubMed1995

Korkormicins, novel depsipeptide antitumor antibiotics from Micromonospora sp C39500: fermentation, precursor directed biosynthesis and biological activities.

Micromonospora sp C39500, isolated in our laboratory from a soil sample, produced a complex of seven novel depsipeptide antitumor antibiotics, designated korkormicins. The major component of the complex, korkormicin A, has a MW of 1452 and a molecular formula of C66H84N16O22. Korkormicin A exhibits potent in vivo antitumor activity against P388 leukemia and M109 lung carcinoma implanted intraperitoneally (ip) in mice, with effective doses of 0.05-0.20 mg kg-1 injection-1, for five or three ip injections, respectively. It is also active against Gram-positive bacteria but inactive against Gram-negative bacteria. The production of korkormicin A was enhanced by 3-fold when 0.1% L-valine was added to the production culture at 48 h. A titer of 401.0 micrograms ml-1 was achieved in the fermenter culture supplemented with 0.1% L-valine.

Animals↗
PubMed1994

Cloning and sequencing of an endo-beta-1,4-glucanase gene mcenA from Micromonospora cellulolyticum 86W-16.

Endo-beta-1,4-glucanase gene mcenA of Micromonospora cellulolyticum 86W-16 was cloned, and the nucleotide sequence was determined. An open reading frame (ORF) of 1374 bases, coding for a peptide (McenA) of 457 amino acids and 46,742 Da, was found. It is preceded by a Gram-positive type of ribosome-binding site and followed by an imperfect inverted repeat. A putative signal peptide containing 23 amino acids is at the N-terminus and a linker region possessing 37 amino acids is in the midpart of McenA. The N-half of McenA functions as the catalytic domain and the C-half might serve as a cellulose-binding domain (CBD). Deletion of the latter did not decrease the CMCase activity of McenA. Significant similarity (70%) was found between the amino acid sequences of McenA and MbcelA, an endoglucanase from Microbispora bispora.

Amino Acid Sequence↗
PubMed2001

The cell wall of Micromonospora purpurea contains a high conductance channel.

In this communication it is demonstrated that the cell wall of the gram-positive bacterium Micromonospora purpurea contains a cell wall channel for the passage of hydrophilic solutes. The channel-forming protein was identified in sucrose step-density-gradient fractions of the cell envelope and in whole cell extracts using either organic solvent or detergent and the lipid bilayer technique. The fractions of the sucrose step-density centrifugation were assayed for NADH-oxidase activity and for the formation of ion-permeable channels in lipid bilayers. The highest NADH-oxidase activity and the highest channel-forming ability were found in different fractions. The cell wall fraction was identified by the presence of meso-diaminopimelic acid and contained an ion-permeable channel with the extremely high single-channel conductance of about 14 nS in 1 M KCl. The channel-forming unit was purified to homogeneity by FPLC on a HiTrap-Q column. It was identified as a heat- and SDS-resistant 200-kDa band on SDS-PAGE and formed the same general diffusion pores in lipid bilayer membranes as those formed by detergent extracts of the cell wall fraction of the sucrose step-density centrifugation. The channels were slightly selective for potassium ions over chloride, possibly caused by an excess of negative charges in or near the channel.

Cell Wall↗
PubMed2005

Differentiation and protease production in Micromonospora echinospora (ATCC 15837).

Micromonospora echinospora differentiates in both submerged and surface cultures producing abundant dark spores after a period of vegetative mycelial growth. In submerged batch cultures, under either carbon or nitrogen limiting conditions, protease activity was found to coincide with sporulation indicating a relationship between proteolytic activity and differentiation in this organism. Further evidence for this link was provided from surface grown cultures wherein sporulation was inhibited by the serine protease inhibitors TLCK and TPCK. The association between proteolysis and differentiation apparent in this organism correlates with evidence of a similar phenomenon observed in the streptomycetes, suggesting that this may be a common response associated with differentiation in filamentous actinomycetes.

Kinetics↗
PubMed1992

Crystallization and preliminary crystallographic study of neuraminidase from Micromonospora viridifaciens.

Single crystals of neuraminidase from the bacterium Micromonospora viridifaciens were obtained using the hanging drop vapour diffusion method and polyethylene glycol as precipitant at pH 5.0 or 5.5. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 48.14 A, b = 82.73 A, c = 84.75 A and with one molecule in the asymmetric unit. Diffraction extends to at least 1.7 A.

Crystallization↗
PubMed1991

Characterisation of aminoglycoside acetyltransferase-encoding genes of neomycin-producing Micromonospora chalcea and Streptomyces fradiae.

Two genes (aac) encoding aminoglycoside-N-acetyltransferase from Streptomyces fradiae and Micromonospora chalcea were cloned: the former identified by hybridization with a homologous gene from Streptomyces rimosus forma paromomycinus, the second by direct expression in Streptomyces lividans using pIJ702 as a vector. These two genes showed pronounced nucleotide and amino acid sequence similarities between themselves and also between previously described streptomycetes aac genes. Comparison of the flanking sequence of actinomycetes aac genes indicates considerable divergence, contrary to the notion that clustered biosynthetic genes for structurally related antibiotics were disseminated in their entirety between microbial species.

Acetyltransferases↗
PubMed1992

Resistance to macrolides and lincosamides in Streptomyces lividans and to aminoglycosides in Micromonospora purpurea.

Ribosomal (r) resistance to gentamicin in clones containing DNA from the producing organism Micromonospora purpurea is determined by grmA, and not by kgmA as originally reported. The kgmA gene originated in Streptomyces tenebrarius and is identical to kgmB. Both grmA and kgm encode enzymes that methylate single specific sites within 16S rRNA, although the site of action of the grmA product has not yet been determined. In either case, the methylated nucleoside is 7-methyl G. Inducible resistance to lincomycin (Ln) and macrolides in Streptomyces lividans TK21 results from expression of two genes: lrm, encoding an rRNA methyltransferase and mgt, encoding a glycosyl transferase (MGT), that specifically inactivates macrolides. The lrm product monomethylates residue A2058 within 23S rRNA (Escherichia coli numbering scheme) and confers high-level resistance to Ln with much lower levels of resistance to macrolides. Substrates for MGT, which utilises UDP-glucose as cofactor, include macrolides with 12-, 14-, 15- or 16-atom cyclic polyketide lactones (as in methymycin, erythromycin, azithromycin or tylosin, respectively) although spiramycin and carbomycin are not apparently modified. The enzyme is specific for the 2'-OH group of saccharide moieties attached to C5 of the 16-atom lactone ring (corresponding to C5 or C3 in 14- or 12-atom lactones, respectively). The lrm and mgt genes have been cloned and sequenced. The deduced lrm product is a 26-kDa protein, similar to other rRNA methyltransferases, such as the carB, tlrA and ermE products, whereas the mgt product (deduced to be 42 kDa) resembles a glycosyl transferase from barley.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1993

Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin) producer, Micromonospora olivasterospora: comparison with other aminoglycoside-resistance-encoding genes.

The nucleotide (nt) sequence of a 3409-bp PvuII fragment carrying the self-defense gene (fmrO) of a fortimicin A (FmA; astromicin) producer, Micromonospora olivasterospora, was determined; four open reading frames (ORFs) exist in this region. Expression analysis of fmrO using the lac promoter in Escherichia coli revealed that ORF-3 encodes fmrO. ORF-1 was considered to encode a FmKH epimerase (fms11). ORF-2, ORF-3 and ORF-4 seemed to form an operon. No homology was detected between fmrO and the resistance-encoding gene fmrT of Streptomyces tenjimariensis, a producer of the Fm-group antibiotic, istamycin. Gene organization around the fmr genes differed considerably between M. olivasterospora and S. tenjimariensis. The deduced amino acid sequence of fmrO showed an identity of 30.8% to grmA of M. purpurea and 35.8% to grmB of M. rosea, respectively, suggesting that fmrO encodes a 16S rRNA methyltransferase. We found in M. purpurea a novel resistance gene distinct from grmA and highly similar to fmrO which conferred a resistance phenotype similar to that of fmrO. These results suggest that fmrO of M. olivasterospora and the two resistance-encoding genes of M. purpurea were derived from a common ancestral gene.

Amino Acid Sequence↗
PubMed1994

Cloning and sequences of two macrolide-resistance-encoding genes from mycinamicin-producing Micromonospora griseorubida.

Two macrolide-resistance determinants were cloned from a mycinamicin (Mm)-producing Micromonospora griseorubida strain in Streptomyces lividans and Streptomyces parvulus. One of the cloned genes, designated myrA, was cloned as a gene which conferred strong resistance to Mm and tylosin (Ty), but not to erythromycin (Er) or josamycin (Jm) on S. lividans. Another gene, named myrB, was cloned as an ErR-encoding gene which conferred MLS resistance (to macrolide, lincosamide and streptogramine B antibiotics) on S. parvulus. Both myrA and myrB were sequenced and the corresponding ORFs were determined. The deduced amino acid (aa) sequence of myrA showed no similarity to proteins in the available databases, suggesting that an unknown mechanism of macrolide resistance is exerted by the MyrA protein. The deduced aa sequence of myrB exhibited high similarity to 23S rRNA methyltransferases (MTases), such as ErmE and CarB, from a variety of microorganisms.

Amino Acid Sequence↗