|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1987-1-7
|
|
pubmed:abstractText |
Binding of guanosine nucleotides to purified native and ADP-ribosylated wheat germ EF-2 was measured. Both forms of EF-2 bound [3H]GDP to the same extent. [3H]GDP binding to native but not to ADP-ribosylated EF-2 was reduced in the presence of GTP and ribosomes. Binding of [gamma-32P]GTP to EF-2 was significantly reduced upon ADP-ribosylation. ADP-ribosylation almost abolished both the stimulatory effect of ribosomes on GTP binding to EF-2 and the ability of EF-2 to form a high-affinity complex with GuoPP(CH2)P and ribosomes. Low-affinity complex formation between EF-2 X GDP and ribosomes was not influenced by ADP-ribosylation. The results indicate that the inhibition of the elongation process caused by the toxin is probably due to the inability of modified EF-2 to exchange GDP with GTP.
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|
pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
24
|
|
pubmed:volume |
208
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
217-20
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1986
|
|
pubmed:articleTitle |
Nucleotide binding to elongation factor 2 inactivated by diphtheria toxin.
|
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|
