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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
27
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pubmed:dateCreated |
1985-12-20
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pubmed:abstractText |
Acanthamoeba actin is the only actin sequenced to date that has neither an NH2-terminal Ac-Asp nor Ac-Glu residue. The protein begins with an Ac-Gly-Asp and is coded for by a gene that specifies a polypeptide beginning Met-Gly-Asp. Thus, the Acanthamoeba actin gene would appear to specify a class II actin with the usual NH2-terminal Cys replaced with a Gly. Previous studies (Rubenstein, P. A., and Martin, D. J. (1983) J. Biol. Chem. 258, 11354-11360) revealed that for class II actins the Met is probably removed early in translation and the Cys is removed post-translationally as an Ac-Cys residue. Two possibilities might explain why Acanthamoeba actin is not processed in a similar fashion. Either Ac-Gly is not a substrate for the enzyme or the enzyme is absent from the organism. To test these alternatives, Acanthamoeba actin was labeled in vivo with [35S]methionine and incubated with processing enzyme from rat liver, rabbit reticulocytes, and Dictyostelium. In no case did the processing reaction occur, indicating that Ac-Gly is not recognized by the enzyme as a substrate. Furthermore, we could not reproducibly detect the presence of a processing enzyme in Acanthamoeba. We were, however, able to show the presence of such an enzyme in Dictyostelium, the first demonstration of this activity in a lower eukaryote.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14857-61
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:4055803-Actins,
pubmed-meshheading:4055803-Amino Acid Sequence,
pubmed-meshheading:4055803-Amoeba,
pubmed-meshheading:4055803-Animals,
pubmed-meshheading:4055803-Dictyostelium,
pubmed-meshheading:4055803-Genes,
pubmed-meshheading:4055803-Methionine,
pubmed-meshheading:4055803-Protein Processing, Post-Translational,
pubmed-meshheading:4055803-Species Specificity
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pubmed:year |
1985
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pubmed:articleTitle |
Lack of NH2-terminal processing of actin from Acanthamoeba castellanii.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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