Garrels, J. I., Hunter, T. (October 1979) Post-translational modification of actins synthesized in vitro. Biochim Biophys Acta, 564 (3). pp. 517-25. ISSN 0006-3002 (Print)0006-3002 (Linking)
Abstract
It has been shown in two different ways that beta and gamma actins synthesized in vitro are acetylated and that the minor species of actin, delta and epsilon, are nonacetylated forms of beta and gamma actin, respectively. Firstly, additon of acetyl-CoA to the wheat germ system translating poly(A)-containing RNA from unfused rat L6 myoblasts, resulted in an increase in the synthesis of beta and gamma actins at the expense of delta and epsilon actins. Secondly, beta and gamma actins were labeled when synthesized in vitro in the presence of [3H]acetyl-CoA. No label was detectable in delta and epsilon actins. By extrapolation this indicates that beta and gamma actin are acetylated in vivo, probably at the N-terminus. beta and gamma actins synthesized in vivo contain a N tau-methylhistidine residue, but no methylation of beta and gamma actins synthesized in vitro was detectable, using S-[3H]adenosylmethionine as a methyl donor.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Acetyl Coenzyme A/metabolism Acetylation Actins/*biosynthesis Animals Cell Line Methionine/metabolism Methylation Muscles Protein Biosynthesis S-Adenosylmethionine/metabolism |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > actin bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > post-translational modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation |
| CSHL Authors: | |
| Communities: | CSHL labs |
| Depositing User: | Matt Covey |
| Date: | 25 October 1979 |
| Date Deposited: | 23 May 2016 16:16 |
| Last Modified: | 23 May 2016 16:16 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/32684 |
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