Linked Life Data

15342235

Source:http://linkedlifedata.com/resource/pubmed/id/15342235

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-9-2
pubmed:databankReference
pubmed:abstractText
The ribosomal L7Ae protein of archaea has the peculiarity to be a component of the C/D and H/ACA snRNPs, that guide rRNA post-transcriptional modifications. Its yeast (Snu13p) and human (15.5kDa protein) homologs are only found in C/D snoRNPs and the (U4/U6, U5) spliceosomal tri-snRNP. By using a large variety of RNAs, we compared the RNA-binding specificities of the recombinant Pyrococcus abyssi L7Ae and Saccharomyces cerevisiae Snu13 proteins. Unlike Snu13p, protein L7Ae binds terminal loops closed by two A:G and G:A pairs and canonical K-turn structures with similar efficiencies, provided that the terminal loop contains at least 5nt. In contrast to Snu13p, binding of protein L7Ae to canonical K-turn structures is not dependent on the identity of the residue at position 2 in the bulge. The peculiar KT-15 motif of P. abyssi 23S rRNA, that is recognized by L7Ae, does not associate with Snu13p. To get more information on the P. abyssi L7Ae protein, we solved its X-ray structure at 1.9A resolution. In spite of their sequence divergence, the free P. abyssi and bound H. marismortui proteins were found to have highly similar structures. Only a limited number of side-chain conformational changes occur at the protein-RNA interface upon RNA binding. In particular, one ion pair that is formed by residues Glu43 and Lys46 in the free protein is disrupted in the ribosomal 50S subunit, so that, residue Glu43 can interact with the RNA residue G264. The Glu43-Lys46 ion pair of protein L7Ae belongs to a complex network of ion pairs that may participate to protein thermostability.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
342
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
757-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15342235-Amino Acid Sequence, pubmed-meshheading:15342235-Archaeal Proteins, pubmed-meshheading:15342235-Base Sequence, pubmed-meshheading:15342235-Binding Sites, pubmed-meshheading:15342235-Haloarcula marismortui, pubmed-meshheading:15342235-Humans, pubmed-meshheading:15342235-Models, Molecular, pubmed-meshheading:15342235-Molecular Sequence Data, pubmed-meshheading:15342235-Nucleic Acid Conformation, pubmed-meshheading:15342235-Protein Conformation, pubmed-meshheading:15342235-Pyrococcus abyssi, pubmed-meshheading:15342235-RNA, Archaeal, pubmed-meshheading:15342235-RNA, Ribosomal, pubmed-meshheading:15342235-Ribonucleoproteins, Small Nuclear, pubmed-meshheading:15342235-Ribosomal Proteins, pubmed-meshheading:15342235-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15342235-Sequence Homology, Amino Acid, pubmed-meshheading:15342235-Static Electricity
pubmed:year
2004
pubmed:articleTitle
The archaeal sRNA binding protein L7Ae has a 3D structure very similar to that of its eukaryal counterpart while having a broader RNA-binding specificity.
pubmed:affiliation
Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, UMR CNRS 7036, Groupe Biocristallographie, Université Henri Poincaré, Nancy I, BP 239, 54506 Vandoeuvre-lès-Nancy, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't