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PMID: 272676 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Ovalbumin: a secreted protein without a transient hydrophobic leader sequence.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 1 ·1978-01-00 ·Pages 94-8

Palmiter RD, Gagnon J, Walsh KA

Abstract

Ovalbumin mRNA was translated in a reticulocyte lysate. The primary translation product starts with methionine derived from Met-tRNAf. When the nascent polypeptide is about 20 residues long, this methionine is removed. The new NH2-terminal glycine is acetylated from acetyl-CoA when the polypeptide is 44 residues long. The sequence of 35 residues at the NH2 terminus of ovalbumin was determined by automated Edman degradation after a method was devised to prevent acetylation during protein synthesis in the reticulocyte lysate. This sequence is the same as that of secreted ovalbumin and does not resemble the transient "signal peptides" associated with most secretory proteins, including three other egg white proteins synthesized in the same cells as ovalbumin.

MeSH Terms
Acetyl Coenzyme A/metabolism Acetylation Amino Acid Sequence Animals Cell-Free System Chickens Female Ovalbumin/biosynthesis,genetics,metabolism Oviducts/metabolism Protein Biosynthesis RNA, Messenger/metabolism
Chemicals
RNA, Messenger Acetyl Coenzyme A Ovalbumin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Palmiter R D
Gagnon J
Walsh K A
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.1.94
Published
1978-01-00
Pages
94-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC411190
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.1.94 PMC Full Text View journal details
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