Literature DB >> 9747670

The protein family of RNA helicases.

A Lüking1, U Stahl, U Schmidt.   

Abstract

RNA helicases represent a large family of proteins that have been detected in almost all biological systems where RNA plays a central role. They are ubiquitously distributed over a wide range of organisms and are involved in nuclear and mitochondrial splicing processes, RNA editing, rRNA processing, translation initiation, nuclear mRNA export, and mRNA degradation. RNA helicases are described as essential factors in cell development and differentiation, and some of them play a role in transcription and replication of viral single-stranded RNA genomes. Comparisons of the conserved sequences reveal a close relationship between them and suggest that these proteins might be derived from a common ancestor. Biochemical studies have revealed a strong dependence of the unwinding activity on ATP hydrolysis. Although RNA helicase activity has only been demonstrated for a few examples yet, it is generally believed that all members of the largest subgroups, the DEAD and DEAH box proteins, exhibit this activity.

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Year:  1998        PMID: 9747670     DOI: 10.1080/10409239891204233

Source DB:  PubMed          Journal:  Crit Rev Biochem Mol Biol        ISSN: 1040-9238            Impact factor:   8.250


  70 in total

1.  Visualization of unwinding activity of duplex RNA by DbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy.

Authors:  Arnon Henn; Ohad Medalia; Shu-Ping Shi; Michal Steinberg; Francois Franceschi; Irit Sagi
Journal:  Proc Natl Acad Sci U S A       Date:  2001-04-10       Impact factor: 11.205

2.  The 100-kda U5 snRNP protein (hPrp28p) contacts the 5' splice site through its ATPase site.

Authors:  N Ismaïli; M Sha; E H Gustafson; M M Konarska
Journal:  RNA       Date:  2001-02       Impact factor: 4.942

3.  Characterization of the cold stress-induced cyanobacterial DEAD-box protein CrhC as an RNA helicase.

Authors:  E Yu; G W Owttrim
Journal:  Nucleic Acids Res       Date:  2000-10-15       Impact factor: 16.971

4.  An mRNA degrading complex in Rhodobacter capsulatus.

Authors:  S Jäger; O Fuhrmann; C Heck; M Hebermehl; E Schiltz; R Rauhut; G Klug
Journal:  Nucleic Acids Res       Date:  2001-11-15       Impact factor: 16.971

5.  Mutagenesis of the Dengue virus type 2 NS3 protein within and outside helicase motifs: effects on enzyme activity and virus replication.

Authors:  A E Matusan; M J Pryor; A D Davidson; P J Wright
Journal:  J Virol       Date:  2001-10       Impact factor: 5.103

6.  Genome-wide gene expression profiles of the developing mouse hippocampus.

Authors:  M Mody; Y Cao; Z Cui; K Y Tay; A Shyong; E Shimizu; K Pham; P Schultz; D Welsh; J Z Tsien
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-03       Impact factor: 11.205

7.  Regularities of context-dependent codon bias in eukaryotic genes.

Authors:  Alexei Fedorov; Serge Saxonov; Walter Gilbert
Journal:  Nucleic Acids Res       Date:  2002-03-01       Impact factor: 16.971

8.  Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA.

Authors:  C M Diges; O C Uhlenbeck
Journal:  EMBO J       Date:  2001-10-01       Impact factor: 11.598

9.  Rearrangement of structured RNA via branch migration structures catalysed by the highly related DEAD-box proteins p68 and p72.

Authors:  O G Rössler; A Straka; H Stahl
Journal:  Nucleic Acids Res       Date:  2001-05-15       Impact factor: 16.971

10.  The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA.

Authors:  C A Tsu; K Kossen; O C Uhlenbeck
Journal:  RNA       Date:  2001-05       Impact factor: 4.942

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