نتایج جستجو برای: like rnase

تعداد نتایج: 661264  

Journal: :Acta crystallographica. Section D, Biological crystallography 2001
J E Kwak J Y Lee B W Han J H Moon S H Sohn I S Park B G Kim S W Suh

The genome of Bacillus subtilis contains three different genes encoding RNase H homologs: RNases HI, HII and HIII. RNase HIII from B. subtilis degrades RNA in RNA-DNA hybrids in an Mg(2+)-dependent manner like Escherichia coli RNase HI. However, they belong to different classes; the former belongs to the 'class II' or 'large' RNase H family, while the latter belongs to the 'class I' or 'small' ...

Journal: :The Journal of biological chemistry 2000
L E Bretscher R L Abel R T Raines

Onconase, a homolog of ribonuclease A (RNase A) with low ribonucleolytic activity, is cytotoxic and has efficacy as a cancer chemotherapeutic. Here variants of RNase A were used to probe the interplay between ribonucleolytic activity and evasion of the cytosolic ribonuclease inhibitor protein (RI) in the cytotoxicity of ribonucleases. K41R/G88R RNase A is a less active catalyst than G88R RNase ...

2012
Asuka Uchida Hidenori Sassa Satoshi Takenaka Yoichi Sakakibara Masahito Suiko Hisato Kunitake

The differences between stylar protein of the Japanese pear (Pyrus pyrifolia (Burm.f.)) cultivars ‘Kosui’ (SS) and ‘Kikusui’ (SS) were compared by two-dimensional difference gel electrophoresis (2-D DIGE), and were labelled and visualized with different fluorescent dyes (IC3-OSu, IC5-OSu) on a single 2-D gel. The individual different expressed proteins spots were subjected to identification. Th...

Journal: :Nucleic acids research 1992
A Vioque

The genes encoding the RNA subunit of ribonuclease P from the unicellular cyanobacterium Synechocystis sp. PCC 6803, and from the heterocyst-forming strains Anabaena sp. PCC 7120 and Calothrix sp. PCC 7601 were cloned using the homologous gene from Anacystis nidulans (Synechococcus sp. PCC 6301) as a probe. The genes and the flanking regions were sequenced. The genes from Anabaena and Calothrix...

Journal: :Molecular cell 2006
Steven M Marquez Julian L Chen Donald Evans Norman R Pace

Ribonuclease P (RNase P) is the ribonucleoprotein endonuclease that processes the 5' ends of precursor tRNAs. Bacterial and eukaryal RNase P RNAs had the same primordial ancestor; however, they were molded differently by evolution. RNase P RNAs of eukaryotes, in contrast to bacterial RNAs, are not catalytically active in vitro without proteins. By comparing the bacterial and eukaryal RNAs, we c...

2011
Sandra C. Viegas Inês J. Silva Margarida Saramago Susana Domingues Cecília M. Arraiano

MicA is a trans-encoded small non-coding RNA, which downregulates porin-expression in stationary-phase. In this work, we focus on the role of endoribonucleases III and E on Salmonella typhimurium sRNA MicA regulation. RNase III is shown to regulate MicA in a target-coupled way, while RNase E is responsible for the control of free MicA levels in the cell. We purified both Salmonella enzymes and ...

2014
Shuvojit Banerjee Arindam Chakrabarti Babal Kant Jha Susan R. Weiss Robert H. Silverman

The interferon (IFN)-inducible antiviral state is mediated in part by the 2',5'-oligoadenylate (2-5A) synthetase (OAS)/RNase L system. 2-5A, produced from ATP by OAS proteins in response to viral double-stranded RNA, binds to and activates RNase L. RNase L restricts viral infections by degrading viral and cellular RNA, inducing autophagy and apoptosis, and producing RNA degradation products tha...

2014
Małgorzata Figiel Marcin Nowotny

RNases H participate in the replication and maintenance of genomic DNA. RNase H1 cleaves the RNA strand of RNA/DNA hybrids, and RNase H2 in addition hydrolyzes the RNA residue of RNA-DNA junctions. RNase H3 is structurally closely related to RNases H2, but its biochemical properties are similar to type 1 enzymes. Its unique N-terminal substrate-binding domain (N-domain) is related to TATA-bindi...

Journal: :Journal of bacteriology 2008
Jing Yang Chaitanya Jain Kurt Schesser

Yersinia spp. use a type 3 secretion system (T3SS) to directly inject six proteins into macrophages, and any impairment of this process results in a profound reduction in virulence. We previously showed that the exoribonuclease polynucleotide phosphorylase (PNPase) was required for optimal T3SS functioning in Yersinia pseudotuberculosis and Yersinia pestis. Here we report that Y. pseudotubercul...

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