Linked Life Data

7548208

Source:http://linkedlifedata.com/resource/pubmed/id/7548208

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-10-23
pubmed:abstractText
Rat liver elongation factor eEF-2 was treated with endoproteinase Glu-C. Two major fragments were obtained, which were identified by N-terminal sequencing and purified. The larger one (F61) contained 554 residues including the N-terminal end, and after a second cleavage released a N-terminal peptide (F7) of 62 residues. The smaller one (F34) contained the other 303 residues including the C terminal end. F61 and F34, either isolated or after combination, were unable to catalyze protein synthesis. However, we show by fluorimetry that F61 could still interact with GTP and GDP. This fragment was was able to participate into a ternary complex with ribosome and GDP, but not with ribosome and a GTP analogue. It was unable to protect the ribosome against ricin-inactivation and to be phosphorylated by the eEF-2-specific Ca(2+)-calmodulin-dependent kinase, though it contained Trp221 and Thr56 involved in these reactions. On the other hand, F34 could be ADP-ribosylated in the presence of NAD+ and diphtheria toxin, but this fragment was apparently unable to bind to ribosomes. These results and those obtained with other proteinases are discussed in the light of the data published recently which show the existence of five different domains in the three-dimensional structure of EF-G.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
1263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Properties of elongation factor-2 fragments obtained by partial proteolysis.
pubmed:affiliation
Laboratoire de Biochimie Médicale, Institut de Biologie et Chimie des Protéines, CNRS, UPR 412, Lyon, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't