نتایج جستجو برای: ribosomal peptide synthetases

تعداد نتایج: 193415  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1997
M Ibba J L Bono P A Rosa D Söll

Lysyl-tRNAs are essential for protein biosynthesis by ribosomal mRNA translation in all organisms. They are synthesized by lysyl-tRNA synthetases (EC 6.1.1.6), a group of enzymes composed of two unrelated families. In bacteria and eukarya, all known lysyl-tRNA synthetases are subclass IIc-type aminoacyl-tRNA synthetases, whereas some archaea have been shown to contain an unrelated class I-type ...

2013
Wen Li Hassan Rokni-Zadeh Matthias De Vleeschouwer Maarten G. K. Ghequire Davy Sinnaeve Guan-Lin Xie Jef Rozenski Annemieke Madder José C. Martins René De Mot

The rhizosphere isolate Pseudomonas putida BW11M1 produces a mixture of cyclic lipopeptide congeners, designated xantholysins. Properties of the major compound xantholysin A, shared with several other Pseudomonas lipopeptides, include antifungal activity and toxicity to Gram-positive bacteria, a supportive role in biofilm formation, and facilitation of surface colonization through swarming. Aty...

Journal: :Microbiology 2007
Deirdre Stack Claire Neville Sean Doyle

In fungi, nonribosomal peptide synthetases (NRP synthetases) are large multi-functional enzymes containing adenylation, thiolation (or peptidyl carrier protein, PCP) and condensation domains. These enzymes are often encoded within gene clusters. Multiple NRP synthetase ORFs have also been identified in fungi (14 in Aspergillus fumigatus). LeaA, a methyltransferase, is involved in secondary meta...

2016
Xunchao Cai Xingxing Kang Huan Xi Changhong Liu Yarong Xue

Bacillus velezensis is a heterotypic synonym of B. methylotrophicus, B. amyloliquefaciens subsp. plantarum, and Bacillus oryzicola, and has been used to control plant fungal diseases. In order to fully understand the genetic basis of antimicrobial capacities, we did a complete genome sequencing of the endophytic B. velezensis strain CC09. Genes tightly associated with biocontrol ability, includ...

Journal: :The EMBO journal 2000
B L Staker P Korber J C Bardwell M A Saper

We have solved the crystal structure of the heat shock protein Hsp15, a newly isolated and very highly inducible heat shock protein that binds the ribosome. Comparison of its structure with those of two RNA-binding proteins, ribosomal protein S4 and threonyl-tRNA synthetase, reveals a novel RNA-binding motif. This newly recognized motif is remarkably common, present in at least eight different ...

2007
Deirdre Stack Claire Neville Sean Doyle

In fungi, nonribosomal peptide synthetases (NRP synthetases) are large multi-functional enzymes containing adenylation, thiolation (or peptidyl carrier protein, PCP) and condensation domains. These enzymes are often encoded within gene clusters. Multiple NRP synthetase ORFs have also been identified in fungi (14 in Aspergillus fumigatus). LeaA, a methyltransferase, is involved in secondary meta...

Journal: :Environmental microbiology 2014
Jolien D'aes Nam Phuong Kieu Valérie Léclère Caroline Tokarski Feyisara Eyiwumi Olorunleke Katrien De Maeyer Philippe Jacques Monica Höfte Marc Ongena

Pseudomonas CMR12a is a biocontrol strain that produces phenazine antibiotics and as yet uncharacterized cyclic lipopeptides (CLPs). The CLPs of CMR12a were studied by chemical structure analysis and in silico analysis of the gene clusters encoding the non-ribosomal peptide synthetases responsible for CLP biosynthesis. CMR12a produces two different classes of CLPs: orfamides B, D and E, whereby...

Abbas Nikravesh Liam Good Majid Sadeghizadeh, Mehrdad Behmanesh

  Background & Objectives: Antisense peptide nucleic acids (PNA) that target growth essential genes show potent bactericidal properties without cell lysis. We considered the possibility that whether PNA treatment influence the bacteria total nucleic acids content and apply approach to develop a new delivery system to Dendritic cells (DCs). DCs are the most potent antigen presenting cells in th...

Journal: :The Journal of biological chemistry 2001
K Eppelmann S Doekel M A Marahiel

Nonribosomal peptides are processed on multifunctional enzymes called nonribosomal peptide synthetases (NRPSs), whose modular multidomain arrangement allowed the rational design of new peptide products. However, the lack of natural competence and efficient transformation methods for most of nonribosomal peptide producer strains prevented the in vivo manipulation of these biosynthetic gene clust...

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