Linked Life Data

10610797

Source:http://linkedlifedata.com/resource/pubmed/id/10610797

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-1-13
pubmed:databankReference
pubmed:abstractText
DEAD-box proteins have been implicated in a wide array of cellular processes ranging from initiation of protein synthesis and ribosome biogenesis to mRNA splicing. Here, we report the isolation, biochemical characterization and crystallization of the first thermophilic DEAD box protein, Hera (heat-resistant RNA-dependent ATPase) from Thermus thermophilus HB8. The molecular mass of the deduced Hera protein sequence (510 amino acid residues) is 55.95 kDa. Hera possesses all of the conserved motifs found among the, DEAD-box RNA helicases. In addition, it also has a motif characteristic of the protein component of ribonuclease P at its C-terminal region (residues 372-386). Hera appears to be non-specific with respect to the RNA species that triggers ATPase activity. Nevertheless, at high temperature, ATPase activity is at a maximum when bacterial 16 S rRNA or 23 S rRNA are used as the substrates. Moreover, a deletion of the RNase P protein motif significantly reduces the ability of Hera to hydrolyze ATP in the presence of RNase P RNA. Hera has a specific ATPase activity of 480 units/microg and therefore, displays the highest ATPase specific activity reported for a protein of the RNA helicase family. We determined that Hera shows helix-destabilizing activity, and that the RNA-unwinding or helix-destabilizing activity of Hera is coupled to ATP hydrolysis. Since Hera is a stable thermophilic protein and we have obtained crystals of it diffracting beyond 2.6 A, the possibilities for structure determination of a full-length RNA-helicase are open.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
795-805
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10610797-Adenosine Triphosphatases, pubmed-meshheading:10610797-Amino Acid Sequence, pubmed-meshheading:10610797-Chromosome Mapping, pubmed-meshheading:10610797-Cloning, Molecular, pubmed-meshheading:10610797-Crystallography, X-Ray, pubmed-meshheading:10610797-Deoxyribonuclease BamHI, pubmed-meshheading:10610797-Endoribonucleases, pubmed-meshheading:10610797-Escherichia coli, pubmed-meshheading:10610797-Escherichia coli Proteins, pubmed-meshheading:10610797-Molecular Sequence Data, pubmed-meshheading:10610797-Protein Conformation, pubmed-meshheading:10610797-RNA, Catalytic, pubmed-meshheading:10610797-RNA, Ribosomal, 16S, pubmed-meshheading:10610797-RNA, Ribosomal, 23S, pubmed-meshheading:10610797-RNA Helicases, pubmed-meshheading:10610797-Ribonuclease P, pubmed-meshheading:10610797-Thermus thermophilus
pubmed:year
1999
pubmed:articleTitle
Hera from Thermus thermophilus: the first thermostable DEAD-box helicase with an RNase P protein motif.
pubmed:affiliation
Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestr. 73, Berlin, D-14195, Germany.
pubmed:publicationType
Journal Article