In vivo NH_2-terminal acetylation of Sindbis virus proteins
- Creators
- Bell, John R.
- Strauss, James H.
Abstract
The in vivo incorporation of exogenous radioactive acetate into two proteins of Sindbis virus, the capsid protein and PE2, is described. Under appropriate labeling conditions, 40-50% of the label in the capsid protein is found in an N-acetyl group which constitutes the NH_2-terminal modification of this blocked protein. The incorporated radiolabeled acetate was useful in the purification and analysis of peptides derived from the NH_2-terminus of the capsid protein, and from these peptides the NH_2-terminal sequence of the protein was determined to be N-acetyl-Met-Asx-, with the asx group most likely asparagine. The analysis of a peptide derived from the NH_2-terminus of PE2 and containing 45% of the acetate-derived label in this protein leads us to conclude that at least a significant fraction of PE2 is also blocked by N-acetylation.
Additional Information
© 1981 American Society for Biochemistry and Molecular Biology. Received for publication, February 13, 1981. We are grateful to Dr. L. E. Hood and his colleagues, in particular Dr. M. W. Hunkapiller, for the use of their equipment and expertise in the separation of peptides by HPLC and the determination of amino acid compositions, to C. M. Rice for his scintillating discussions during the course of this work, and to E. M. Lenches for expert technical assistance and conscientiously growing large amounts of unlabeled virus. This work was supported by Grants GM06965 and A110793 from the National Institutes of Health and by Grant PCM80-22830 from the National Science Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. John R. Bell - Supported by Training Grant GM00086 from the National Institutes of Health.Attached Files
Published - J._Biol._Chem.-1981-Bell-8006-11.pdf
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Additional details
- Eprint ID
- 68554
- Resolver ID
- CaltechAUTHORS:20160620-164128017
- NIH
- GM-06965
- NIH
- AI-10793
- NSF
- PCM80-22830
- NIH Predoctoral Fellowship
- GM-00086
- Created
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2016-06-22Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field