scholarly journals The gene cluster of aureocyclicin 4185: the first cyclic bacteriocin of Staphylococcus aureus

Microbiology ◽  
2014 ◽  
Vol 160 (5) ◽  
pp. 917-928 ◽  
Author(s):  
Amina Potter ◽  
Hilana Ceotto ◽  
Marcus Lívio Varella Coelho ◽  
Allan J. Guimarães ◽  
Maria do Carmo de Freire Bastos
Keyword(s):  
Staphylococcus Aureus ◽  
Gene Cluster ◽  
Homology Modelling ◽  
Gene Clusters ◽  
Bacteriocin Production ◽  
Encoding Gene ◽  
Membrane Spanning ◽  
Carnocyclin A ◽  
Membrane Spanning Domains ◽  
Bacteriocin Gene

Staphylococcus aureus 4185 was previously shown to produce at least two bacteriocins. One of them is encoded by pRJ101. To detect the bacteriocin-encoding gene cluster, an ~9160 kb region of pRJ101 was sequenced. In silico analyses identified 10 genes (aclX, aclB, aclI, aclT, aclC, aclD, aclA, aclF, aclG and aclH) that might be involved in the production of a novel cyclic bacteriocin named aureocyclicin 4185. The organization of these genes was quite similar to that of the gene cluster responsible for carnocyclin A production and immunity. Four putative proteins encoded by these genes (AclT, AclC, AclD and AclA) also exhibited similarity to proteins encoded by cyclic bacteriocin gene clusters. Mutants derived from insertion of Tn917-lac into aclC, aclF, aclH and aclX were affected in bacteriocin production and growth. AclX is a 205 aa putative protein not encoded by the gene clusters of other cyclic bacteriocins. AclX exhibits 50 % similarity to a permease and has five putative membrane-spanning domains. Transcription analyses suggested that aclX is part of the aureocyclicin 4185 gene cluster, encoding a protein required for bacteriocin production. The aclA gene is the structural gene of aureocyclicin 4185, which shows 65 % similarity to garvicin ML. AclA is proposed to be cleaved off, generating a mature peptide with a predicted M r of 5607 Da (60 aa). By homology modelling, AclA presents four α-helices, like carnocyclin A. AclA could not be found at detectable levels in the culture supernatant of a strain carrying only pRJ101. To our knowledge, this is the first report of a cyclic bacteriocin gene cluster in the genus Staphylococcus.

scholarly journals Glycosulfatase-Encoding Gene Cluster in Bifidobacterium breve UCC2003

2016 ◽  
Vol 82 (22) ◽  
pp. 6611-6623 ◽  
Author(s):  
Muireann Egan ◽  
Hao Jiang ◽  
Mary O'Connell Motherway ◽  
Stefan Oscarson ◽  
Douwe van Sinderen
Keyword(s):  
Gastrointestinal Tract ◽  
Gut Microbiota ◽  
Gene Cluster ◽  
Digestive Tract ◽  
Gene Clusters ◽  
Content Type ◽  
Reading Frame ◽  
Bifidobacterium Breve ◽  
Breastfed Infants ◽  
Encoding Gene

ABSTRACTBifidobacteria constitute a specific group of commensal bacteria typically found in the gastrointestinal tract (GIT) of humans and other mammals.Bifidobacterium brevestrains are numerically prevalent among the gut microbiota of many healthy breastfed infants. In the present study, we investigated glycosulfatase activity in a bacterial isolate from a nursling stool sample,B. breveUCC2003. Two putative sulfatases were identified on the genome ofB. breveUCC2003. The sulfated monosaccharideN-acetylglucosamine-6-sulfate (GlcNAc-6-S) was shown to support the growth ofB. breveUCC2003, whileN-acetylglucosamine-3-sulfate,N-acetylgalactosamine-3-sulfate, andN-acetylgalactosamine-6-sulfate did not support appreciable growth. By using a combination of transcriptomic and functional genomic approaches, a gene cluster designatedats2was shown to be specifically required for GlcNAc-6-S metabolism. Transcription of theats2cluster is regulated by a repressor open reading frame kinase (ROK) family transcriptional repressor. This study represents the first description of glycosulfatase activity within theBifidobacteriumgenus.IMPORTANCEBifidobacteria are saccharolytic organisms naturally found in the digestive tract of mammals and insects.Bifidobacterium brevestrains utilize a variety of plant- and host-derived carbohydrates that allow them to be present as prominent members of the infant gut microbiota as well as being present in the gastrointestinal tract of adults. In this study, we introduce a previously unexplored area of carbohydrate metabolism in bifidobacteria, namely, the metabolism of sulfated carbohydrates.B. breveUCC2003 was shown to metabolizeN-acetylglucosamine-6-sulfate (GlcNAc-6-S) through one of two sulfatase-encoding gene clusters identified on its genome. GlcNAc-6-S can be found in terminal or branched positions of mucin oligosaccharides, the glycoprotein component of the mucous layer that covers the digestive tract. The results of this study provide further evidence of the ability of this species to utilize mucin-derived sugars, a trait which may provide a competitive advantage in both the infant gut and adult gut.

scholarly journals Targeted induction of a silent fungal gene cluster encoding the bacteria-specific germination inhibitor fumigermin

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Maria Cristina Stroe ◽  
Tina Netzker ◽  
Kirstin Scherlach ◽  
Thomas Krüger ◽  
Christian Hertweck ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Polyketide Synthase ◽  
Biological Activities ◽  
Gene Clusters ◽  
Ecological Function ◽  
The Novel ◽  
Ecological Context ◽  
Fungal Metabolite ◽  
Silent Gene ◽  
Encoding Gene

Microorganisms produce numerous secondary metabolites (SMs) with various biological activities. Many of their encoding gene clusters are silent under standard laboratory conditions because for their activation they need the ecological context, such as the presence of other microorganisms. The true ecological function of most SMs remains obscure, but understanding of both the activation of silent gene clusters and the ecological function of the produced compounds is of importance to reveal functional interactions in microbiomes. Here, we report the identification of an as-yet uncharacterized silent gene cluster of the fungus Aspergillus fumigatus, which is activated by the bacterium Streptomyces rapamycinicus during the bacterial-fungal interaction. The resulting natural product is the novel fungal metabolite fumigermin, the biosynthesis of which requires the polyketide synthase FgnA. Fumigermin inhibits germination of spores of the inducing S. rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor.

scholarly journals Distribution and Genetic Diversity of Bacteriocin Gene Clusters in Rumen Microbial Genomes

2015 ◽  
Vol 81 (20) ◽  
pp. 7290-7304 ◽  
Author(s):  
Analice C. Azevedo ◽  
Cláudia B. P. Bento ◽  
Jeronimo C. Ruiz ◽  
Marisa V. Queiroz ◽  
Hilário C. Mantovani
Keyword(s):  
Antimicrobial Peptides ◽  
Bacterial Species ◽  
Gene Clusters ◽  
Class Ii ◽  
Bacteriocin Production ◽  
Class Iii ◽  
Genome Sequences ◽  
Ruminal Bacteria ◽  
Content Type ◽  
Bacteriocin Gene

ABSTRACTSome species of ruminal bacteria are known to produce antimicrobial peptides, but the screening procedures have mostly been based onin vitroassays using standardized methods. Recent sequencing efforts have made available the genome sequences of hundreds of ruminal microorganisms. In this work, we performed genome mining of the complete and partial genome sequences of 224 ruminal bacteria and 5 ruminal archaea to determine the distribution and diversity of bacteriocin gene clusters. A total of 46 bacteriocin gene clusters were identified in 33 strains of ruminal bacteria. Twenty gene clusters were related to lanthipeptide biosynthesis, while 11 gene clusters were associated with sactipeptide production, 7 gene clusters were associated with class II bacteriocin production, and 8 gene clusters were associated with class III bacteriocin production. The frequency of strains whose genomes encode putative antimicrobial peptide precursors was 14.4%. Clusters related to the production of sactipeptides were identified for the first time among ruminal bacteria. BLAST analysis indicated that the majority of the gene clusters (88%) encoding putative lanthipeptides contained all the essential genes required for lanthipeptide biosynthesis. Most strains ofStreptococcus(66.6%) harbored complete lanthipeptide gene clusters, in addition to an open reading frame encoding a putative class II bacteriocin. Albusin B-like proteins were found in 100% of theRuminococcus albusstrains screened in this study. Thein silicoanalysis provided evidence of novel biosynthetic gene clusters in bacterial species not previously related to bacteriocin production, suggesting that the rumen microbiota represents an underexplored source of antimicrobial peptides.

scholarly journals Functional Analysis of the Gene Cluster Involved in Production of the Bacteriocin Circularin A by Clostridium beijerinckii ATCC 25752

2003 ◽  
Vol 69 (10) ◽  
pp. 5839-5848 ◽  
Author(s):  
Robèr Kemperman ◽  
Marnix Jonker ◽  
Arjen Nauta ◽  
Oscar P. Kuipers ◽  
Jan Kok
Keyword(s):  
Bacteriocin Production ◽  
Clostridium Beijerinckii ◽  
Open Reading Frames ◽  
Atp Binding ◽  
Additional Resistance ◽  
Membrane Spanning ◽  
Overlapping Open Reading Frames ◽  
Atp Binding Protein ◽  
Membrane Spanning Domains ◽  
Reading Frames

ABSTRACT A region of 12 kb flanking the structural gene of the cyclic antibacterial peptide circularin A of Clostridium beijerinckii ATCC 25752 was sequenced, and the putative proteins involved in the production and secretion of circularin A were identified. The genes are tightly organized in overlapping open reading frames. Heterologous expression of circularin A in Enterococcus faecalis was achieved, and five genes were identified as minimally required for bacteriocin production and secretion. Two of the putative proteins, CirB and CirC, are predicted to contain membrane-spanning domains, while CirD contains a highly conserved ATP-binding domain. Together with CirB and CirC, this ATP-binding protein is involved in the production of circularin A. The fifth gene, cirE, confers immunity towards circularin A when expressed in either Lactococcus lactis or E. faecalis and is needed in order to allow the bacteria to produce bacteriocin. Additional resistance against circularin A is conferred by the activity of the putative transporter consisting of CirB and CirD.

Characterization of a gene cluster encoding the maleylacetate reductase from Ralstonia eutropha 335T, an enzyme recruited for growth with 4-fluorobenzoate

Microbiology ◽  
2004 ◽  
Vol 150 (2) ◽  
pp. 463-472 ◽  
Author(s):  
Volker Seibert ◽  
Monika Thiel ◽  
Isabelle-S. Hinner ◽  
Michael Schlömann
Keyword(s):  
Gene Cluster ◽  
Burkholderia Cepacia ◽  
Ralstonia Eutropha ◽  
Regulatory Gene ◽  
Gene Clusters ◽  
Reductase Gene ◽  
Maleylacetate Reductase ◽  
Encoding Gene

A gene cluster containing a gene for maleylacetate reductase (EC 1.3.1.32) was cloned from Ralstonia eutropha 335T (DSM 531T), which is able to utilize 4-fluorobenzoate as sole carbon source. Sequencing of this gene cluster showed that the R. eutropha 335T maleylacetate reductase gene, macA, is part of a novel gene cluster, which is not related to the known maleylacetate-reductase-encoding gene clusters. It otherwise comprises a gene for a hypothetical membrane transport protein, macB, possibly co-transcribed with macA, and a presumed regulatory gene, macR, which is divergently transcribed from macBA. MacA was found to be most closely related to TftE, the maleylacetate reductase from Burkholderia cepacia AC1100 (62 % identical positions) and to a presumed maleylacetate reductase from a dinitrotoluene catabolic gene cluster from B. cepacia R34 (61 % identical positions). By expressing macA in Escherichia coli, it was confirmed that macA encodes a functional maleylacetate reductase. Purification of maleylacetate reductase from 4-fluorobenzoate-grown R. eutropha 335T cells allowed determination of the N-terminal sequence of the purified protein, which was shown to be identical to that predicted from the cloned macA gene, thus proving that the gene is, in fact, recruited for growth of R. eutropha 335T with this substrate.

scholarly journals Draft Genome Sequence of Staphylococcus aureus 4185, a Strain That Produces Aureocyclicin 4185

2017 ◽  
Vol 5 (44) ◽  
Author(s):  
Márcia Silva Francisco ◽  
Felipe Miceli Farias ◽  
Ilana Nascimento Sousa Santos ◽  
Selda Loase Salustiano Marques-Bastos ◽  
Rodolpho Mattos Albano ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Gene Cluster ◽  
Genome Sequence ◽  
Genome Analysis ◽  
Draft Genome ◽  
Complete Sequence ◽  
Bacterial Chromosome ◽  
Draft Genome Sequence ◽  
Content Type ◽  
Bacteriocin Gene

ABSTRACT The draft genome sequence of the aureocyclicin 4185-producing strain Staphylococcus aureus 4185 is presented. The assembly contains 2,789,721 bp and a G+C content of 32.8%. Genome analysis allowed us to determine the complete sequence of the bacteriocinogenic plasmid pRJ101 and to find another bacteriocin gene cluster encoded on the bacterial chromosome.

Complete genome of mangrove-derived anti-MRSA streptomycete, Streptomyces pluripotens MUSC 135T

2018 ◽  
Vol 1 (1) ◽  
Author(s):  
Hooi-Leng Ser ◽  
Kok-Gan Chan ◽  
Wen-Si Tan ◽  
Wai-Fong Yin ◽  
Bey-Hing Goh ◽  
...  
Keyword(s):  
Complete Genome ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Gene Clusters ◽  
Salmonella Typhi ◽  
Bacteriocin Production ◽  
Trna Genes ◽  
Genus Streptomyces ◽  
Mining Tool ◽  
Bioactive Potential ◽  
Effective Drugs

Microorganisms serve as attractive resources, owing to their ability to synthesize structurally-diverse substanceswith various bioactivities. Within the Bacteria domain, members of the genus Streptomyces have demonstrated remarkableability to produce clinically useful, secondary metabolites such as anticancer, antioxidants, antivirals and antibacterials.Streptomyces pluripotens MUSC 135T was isolated as novel strain from mangrove forest in Malaysia. This strain exhibitedbroad spectrum bacteriocin against several pathogens including methicillin-resistant Staphylococcus aureus (MRSA) strainATCC BAA-44, Salmonella typhi ATCC 19430T and Aeromonas hydrophila ATCC 7966T. Thus, the strain was selected forwhole genome sequencing as an attempt to explore its bioactive potential. Here we report the first complete genome of S.pluripotens MUSC 135T genome which comprise of 7.35 Mbp with G+C content of 69.9 %. A total of 6,404 open readingframes (ORFs) were predicted, along with 18 rRNA and 69 tRNA genes. Using bacteriocin mining tool, BAGEL detectedeights gene clusters associated with bacteriocin production including lanthipeptides and linear azol(in)e-containing peptides(LAPs). Members of Streptomyces have contributed greatly towards improving lives, particularly against deadly infectionsand chronic diseases. The availability of S. pluripotens MUSC 135T genome sequence has opened new window for drugdiscovery, particularly for effective drugs against harmful pathogens such as MRSA and certainly deserves further detailedstudy.

scholarly journals GIT1, a Gene Encoding a Novel Transporter for Glycerophosphoinositol in Saccharomyces cerevisiae

Genetics ◽  
1998 ◽  
Vol 149 (4) ◽  
pp. 1707-1715 ◽  
Author(s):  
J L Patton-Vogt ◽  
S A Henry
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Regulatory Gene ◽  
Sugar Transport ◽  
Open Reading Frame ◽  
Gene Encoding ◽  
Reading Frame ◽  
Membrane Spanning ◽  
Membrane Spanning Domains ◽  
Uptake And Metabolism ◽  
Cells Cultured

Abstract Phosphatidylinositol catabolism in Saccharomyces cerevisiae cells cultured in media containing inositol results in the release of glycerophosphoinositol (GroPIns) into the medium. As the extracellular concentration of inositol decreases with growth, the released GroPIns is transported back into the cell. Exploiting the ability of the inositol auxotroph, ino1, to use exogenous GroPIns as an inositol source, we have isolated mutants (Git−) defective in the uptake and metabolism of GroPIns. One mutant was found to be affected in the gene encoding the transcription factor, SPT7. Mutants of the positive regulatory gene INO2, but not of its partner, INO4, also have the Git− phenotype. Another mutant was complemented by a single open reading frame (ORF) termed GIT1 (glycerophosphoinositol). This ORF consists of 1556 bp predicted to encode a polypeptide of 518 amino acids and 57.3 kD. The predicted Git1p has similarity to a variety of S. cerevisiae transporters, including a phosphate transporter (Pho84p), and both inositol transporters (Itr1p and Itr2p). Furthermore, Git1p contains a sugar transport motif and 12 potential membrane-spanning domains. Transport assays performed on a git1 mutant together with the above evidence indicate that the GIT1 gene encodes a permease involved in the uptake of GroPIns.

scholarly journals Structural comparison of Acinetobacter baumannii β-ketoacyl-acyl carrier protein reductases in fatty acid and aryl polyene biosynthesis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Woo Cheol Lee ◽  
Sungjae Choi ◽  
Ahjin Jang ◽  
Kkabi Son ◽  
Yangmee Kim
Keyword(s):  
Fatty Acid ◽  
Acinetobacter Baumannii ◽  
Gene Cluster ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Gene Clusters ◽  
Carrier Protein ◽  
Aryl Group ◽  
Visible Absorption

AbstractSome Gram-negative bacteria harbor lipids with aryl polyene (APE) moieties. Biosynthesis gene clusters (BGCs) for APE biosynthesis exhibit striking similarities with fatty acid synthase (FAS) genes. Despite their broad distribution among pathogenic and symbiotic bacteria, the detailed roles of the metabolic products of APE gene clusters are unclear. Here, we determined the crystal structures of the β-ketoacyl-acyl carrier protein (ACP) reductase ApeQ produced by an APE gene cluster from clinically isolated virulent Acinetobacter baumannii in two states (bound and unbound to NADPH). An in vitro visible absorption spectrum assay of the APE polyene moiety revealed that the β-ketoacyl-ACP reductase FabG from the A. baumannii FAS gene cluster cannot be substituted for ApeQ in APE biosynthesis. Comparison with the FabG structure exhibited distinct surface electrostatic potential profiles for ApeQ, suggesting a positively charged arginine patch as the cognate ACP-binding site. Binding modeling for the aryl group predicted that Leu185 (Phe183 in FabG) in ApeQ is responsible for 4-benzoyl moiety recognition. Isothermal titration and arginine patch mutagenesis experiments corroborated these results. These structure–function insights of a unique reductase in the APE BGC in comparison with FAS provide new directions for elucidating host–pathogen interaction mechanisms and novel antibiotics discovery.

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