Lack of NH2-terminal processing of actin from Acanthamoeba castellanii

Kent L Redman; Debra J Martin; Edward D Korn; Peter A Rubenstein

doi:10.1016/S0021-9258(17)38651-9

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Lack of NH2-terminal processing of actin from Acanthamoeba castellanii

Journal article

Open access

Peer reviewed

Lack of NH2-terminal processing of actin from Acanthamoeba castellanii

Kent L Redman, Debra J Martin, Edward D Korn and Peter A Rubenstein

The Journal of biological chemistry, Vol.260(27), pp.14857-14861

11/25/1985

DOI: 10.1016/S0021-9258(17)38651-9

PMID: 4055803

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Abstract

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.

Genes

Amino Acid Sequence

Actins - biosynthesis

Actins - isolation & purification

Animals

Species Specificity

Methionine - metabolism

Dictyostelium - genetics

Protein Processing, Post-Translational

Amoeba - metabolism

Dictyostelium - metabolism

Actins - genetics

Details

Title: Subtitle: Lack of NH2-terminal processing of actin from Acanthamoeba castellanii
Creators: Kent L Redman
Debra J Martin
Edward D Korn
Peter A Rubenstein
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.260(27), pp.14857-14861
DOI: 10.1016/S0021-9258(17)38651-9
PMID: 4055803
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: GM-33689 / NIGMS NIH HHS
Language: English
Date published: 11/25/1985
Academic Unit: Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984024542202771

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