Cargando…

Substrate Recognition and Modification by the Nosiheptide Resistance Methyltransferase

BACKGROUND: The proliferation of antibiotic resistant pathogens is an increasing threat to the general public. Resistance may be conferred by a number of mechanisms including covalent or mutational modification of the antibiotic binding site, covalent modification of the drug, or the over-expression...

Descripción completa

Detalles Bibliográficos
Autores principales:	Yin, Sitao, Jiang, Hengyi, Chen, Dongrong, Murchie, Alastair I. H.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2015
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4409310/ https://www.ncbi.nlm.nih.gov/pubmed/25910005 http://dx.doi.org/10.1371/journal.pone.0122972

Ejemplares similares

Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe
por: Jiang, Hengyi, et al.
Publicado: (2011)

The function of twister ribozyme variants in non-LTR retrotransposition in Schistosoma mansoni
por: Liu, Getong, et al.
Publicado: (2021)

Activity of the thiopeptide antibiotic nosiheptide against contemporary strains of methicillin-resistant Staphylococcus aureus
por: Haste, Nina M., et al.
Publicado: (2012)

A novel function of the mitochondrial transcription factor Mtf1 in fission yeast; Mtf1 regulates the nuclear transcription of srk1
por: Sun, Wenxia, et al.
Publicado: (2011)

In vitro and intracellular inhibitory activities of nosiheptide against Mycobacterium abscessus
por: Zhu, Rui, et al.
Publicado: (2022)

Nosiheptide Harbors Potent In Vitro and Intracellular Inhbitory Activities against Mycobacterium tuberculosis
por: Yu, Xia, et al.
Publicado: (2022)

The Global Transcriptional Response of Fission Yeast to Hydrogen Sulfide
por: Jia, Xu, et al.
Publicado: (2011)

Structure-based Mechanistic Insights into Terminal Amide Synthase in Nosiheptide-Represented Thiopeptides Biosynthesis
por: Liu, Shanshan, et al.
Publicado: (2015)

Design of a chimeric glycosyltransferase OleD for the site‐specific O‐monoglycosylation of 3‐hydroxypyridine in nosiheptide
por: Zhao, Ling, et al.
Publicado: (2023)

Genome-wide identification of Kanamycin B binding RNA in Escherichia coli
por: Chang, Yaowen, et al.
Publicado: (2023)

Interactions between SAM and the 5′ UTR mRNA of the sam1 gene regulate translation in S. pombe
por: Zhang, Xuhui, et al.
Publicado: (2020)

Interactions between the 5′ UTR mRNA of the spe2 gene and spermidine regulate translation in S. pombe
por: Sun, Wenxia, et al.
Publicado: (2020)

Discovery of Nosiheptide, Griseoviridin, and Etamycin as Potent Anti-Mycobacterial Agents against Mycobacterium avium Complex
por: Hosoda, Kanji, et al.
Publicado: (2019)

Biosynthesis of the nosiheptide indole side ring centers on a cryptic carrier protein NosJ
por: Ding, Wei, et al.
Publicado: (2017)

Transcriptome profiling in response to Kanamycin B reveals its wider non-antibiotic cellular function in Escherichia coli
por: Chang, Yaowen, et al.
Publicado: (2022)

Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases
por: Strassler, Sarah E., et al.
Publicado: (2022)

Structural basis for substrate recognition by the human N-terminal methyltransferase 1
por: Dong, Cheng, et al.
Publicado: (2015)

Genome-wide systematic identification of methyltransferase recognition and modification patterns
por: Jensen, Torbjørn Ølshøj, et al.
Publicado: (2019)

Osmium tetroxide as a probe of RNA structure
por: Zhang, Jing, et al.
Publicado: (2017)

Aminoglycoside riboswitch control of the expression of integron associated aminoglycoside resistance adenyltransferases
por: Zhang, Jun, et al.
Publicado: (2020)

Rerouting the Pathway for the Biosynthesis of the Side Ring System of Nosiheptide: The Roles of NosI, NosJ, and NosK
por: Badding, Edward D., et al.
Publicado: (2017)

Effect Analysis of Mineral Salt Concentrations on Nosiheptide Production by Streptomyces actuosus Z-10 Using Response Surface Methodology
por: Zhou, Wei, et al.
Publicado: (2014)

30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC
por: Srinivas, Pooja, et al.
Publicado: (2023)

50S subunit recognition and modification by the Mycobacterium tuberculosis ribosomal RNA methyltransferase TlyA
por: Laughlin, Zane T., et al.
Publicado: (2022)

Probabilistic Approach to Predicting Substrate Specificity of Methyltransferases
por: Szczepińska, Teresa, et al.
Publicado: (2014)

Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2′-O-methyltransferase
por: Zhou, Mi, et al.
Publicado: (2015)

Unexpected expansion of tRNA substrate recognition by the yeast m(1)G(9) methyltransferase Trm10
por: Swinehart, William E., et al.
Publicado: (2013)

In vitro analysis of phosphorothioate modification of DNA reveals substrate recognition by a multiprotein complex
por: Cao, Bo, et al.
Publicado: (2015)

Structural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD
por: Jiang, Yiyang, et al.
Publicado: (2017)

Identification of nonhistone substrates of the lysine methyltransferase PRDM9
por: Hanquier, Jocelyne N., et al.
Publicado: (2023)

Computational Investigation of the Interplay of Substrate Positioning and Reactivity in Catechol O-Methyltransferase
por: Patra, Niladri, et al.
Publicado: (2016)

Crystal structures of PigF, an O-methyltransferase involved in the prodigiosin synthetic pathway, reveal an induced-fit substrate-recognition mechanism
por: Qiu, Shenshen, et al.
Publicado: (2022)

Protein arginine methyltransferase 6 is a novel substrate of protein arginine methyltransferase 1
por: Cao, Meng-Tong, et al.
Publicado: (2023)

Assembly and substrate recognition of curli biogenesis system
por: Yan, Zhaofeng, et al.
Publicado: (2020)

A Chemical Method for Labeling Lysine Methyltransferase Substrates
por: Binda, Olivier, et al.
Publicado: (2011)

Substrate Profiling of Anion Methyltransferases for Promiscuous Synthesis of S‐Adenosylmethionine Analogs from Haloalkanes
por: Schülke, Kai H., et al.
Publicado: (2022)

Hypoxia-Inducible Lysine Methyltransferases: G9a and GLP Hypoxic Regulation, Non-histone Substrate Modification, and Pathological Relevance
por: Chopra, Anand, et al.
Publicado: (2020)

tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily
por: Liu, Ru-Juan, et al.
Publicado: (2015)

Substrate Plasticity of a Fungal Peptide α-N-Methyltransferase
por: Song, Haigang, et al.
Publicado: (2020)

Biochemical and Computational Analysis of the Substrate Specificities of Cfr and RlmN Methyltransferases
por: Ntokou, Eleni, et al.
Publicado: (2015)

Cannot write session to /tmp/vufind_sessions/sess_8400l5d7ea9j5pgc8k9igjbus4