Literature DB >> 16232566

Molecular diversities of RNases H.

N Ohtani1, M Haruki, M Morikawa, S Kanaya.   

Abstract

RNase H is an enzyme that specifically cleaves RNA hybridized to DNA. The enzyme is ubiquitously present in various organisms. Single bacterial and eucaryotic cells often contain two RNases H, whereas single archaeal cells contain only one. To determine whether there is a physiological significance in the ubiquity and multiplicity of the enzyme, and whether all enzymes are evolutionarily diverged from a common ancestor, we carried out phylogenetic analyses of the RNase H sequences. In this report, we demonstrated that RNases H are classified into two major families, Type 1 and Type 2 RNases H, of which only the Type 2 enzymes are present in all living organisms, including bacteria, archaea, and eucaryotes, suggesting that they represent an ancestral form of RNases H. Based on this information, we discuss the evolutionary relationships and possible cellular functions of RNases H.

Year:  1999        PMID: 16232566     DOI: 10.1016/s1389-1723(99)80168-6

Source DB:  PubMed          Journal:  J Biosci Bioeng        ISSN: 1347-4421            Impact factor:   2.894


  32 in total

1.  Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses.

Authors:  A Muroya; D Tsuchiya; M Ishikawa; M Haruki; M Morikawa; S Kanaya; K Morikawa
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

2.  Expression of Moloney murine leukemia virus RNase H rescues the growth defect of an Escherichia coli mutant.

Authors:  A G Campbell
Journal:  J Virol       Date:  2001-07       Impact factor: 5.103

3.  Structure-specific nuclease activities of Pyrococcus abyssi RNase HII.

Authors:  Sébastien Le Laz; Audrey Le Goaziou; Ghislaine Henneke
Journal:  J Bacteriol       Date:  2010-05-14       Impact factor: 3.490

4.  Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.

Authors:  Harriet A Watkins; Edward N Baker
Journal:  J Bacteriol       Date:  2010-04-02       Impact factor: 3.490

5.  Crystallization and preliminary crystallographic analysis of type 1 RNase H from the hyperthermophilic archaeon Sulfolobus tokodaii 7.

Authors:  Dong Ju You; Hyongi Chon; Yuichi Koga; Kazufumi Takano; Shigenori Kanaya
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-07-25

6.  Crystallization and preliminary X-ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilus.

Authors:  Hyongi Chon; Hiroyoshi Matsumura; Yuichi Koga; Kazufumi Takano; Shigenori Kanaya
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-02-12

7.  Substrate Specificity for Bacterial RNases HII and HIII Is Influenced by Metal Availability.

Authors:  Justin R Randall; William G Hirst; Lyle A Simmons
Journal:  J Bacteriol       Date:  2018-01-24       Impact factor: 3.490

Review 8.  The Clash of Macromolecular Titans: Replication-Transcription Conflicts in Bacteria.

Authors:  Kevin S Lang; Houra Merrikh
Journal:  Annu Rev Microbiol       Date:  2018-06-01       Impact factor: 15.500

9.  Replication-Transcription Conflicts Generate R-Loops that Orchestrate Bacterial Stress Survival and Pathogenesis.

Authors:  Kevin S Lang; Ashley N Hall; Christopher N Merrikh; Mark Ragheb; Hannah Tabakh; Alex J Pollock; Joshua J Woodward; Julia E Dreifus; Houra Merrikh
Journal:  Cell       Date:  2017-08-10       Impact factor: 41.582

Review 10.  Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding.

Authors:  Atsushi Mukaiyama; Kazufumi Takano
Journal:  Int J Mol Sci       Date:  2009-03-24       Impact factor: 6.208

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.