Linked Life Data

2125480

Source:http://linkedlifedata.com/resource/pubmed/id/2125480

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1991-2-25
pubmed:abstractText
Translational initiation factor IF-2 is involved in a multistep pathway leading to the synthesis of the first peptide bond. IF-2 is a guanine nucleotide binding protein (G-protein) and catalyzes GTP hydrolysis in the presence of ribosomes. According to sequence homologies with other G-proteins, particularly EF-Tu, a theoretical model for the tertiary structure of the putative G-domain of IF-2 has been previously proposed [Cenatiempo, Y., Deville, F., Dondon, J., Grunberg-Manago, M., Hershey, J. W. B., Hansen, H. F., Petersen, H. U., Clark, B. F. C., Kjeldgaard, M., La Cour, T. F. M., Mortensen, K. K., & Nyborg, J. (1987) Biochemistry 26, 5070-5076]. A short fragment of IF-2 encompassing the putative G-domain was purified by limited proteolysis of a chimeric protein, synthesized from a gene fusion, between a segment of the IF-2 gene and lacZ. The N- and C-terminal sequences of this IF-2 peptide were characterized. Its calculated length is 181 amino acids and its molecular mass 19.4 kDa, whereas it migrates at 14 kDa in SDS-polyacrylamide gels. This segment of IF-2 can form binary complexes with GDP and can be cross-linked to GTP, therefore indicating that it really corresponds to the G-domain. However, in contrast to the situation described for the purified G-domain of EF-Tu, the IF-2 fragment did not hydrolyze GTP even in the presence of ribosomes. It is assumed that active centers of IF-2 located outside the G-domain are needed for the latter reaction.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9728-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purified internal G-domain of translational initiation factor IF-2 displays guanine nucleotide binding properties.
pubmed:affiliation
Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't