In:
Science, American Association for the Advancement of Science (AAAS), Vol. 327, No. 5968 ( 2010-02-19), p. 966-967
Abstract:
Acetylation of the amino terminus (Nt-acteylation) of a protein is one of the most common modifications, occurring in about 50% of yeast proteins and more than 80% of human proteins ( 1 ). It is catalyzed by N-terminal acetyltransferases, occurs predominantly on a nascent polypeptide chain as it is synthesized, and seems to be irreversible. So far, the biological role of Nt-acetylation has been enigmatic; only in a few cases has it been reported to affect protein functionality [for instance, nonacetylated actin is less efficient at assembling microfilaments ( 2 )]. Controlling the activity of individual proteins cannot, however, explain the massive Nt-acetylation of bulk proteins. On page 973 in this issue, Hwang et al. ( 3 ) demonstrate that acetylation of the amino terminus of a protein can function as a degration signal (degron), revealing an entirely unexpected role of acetylation in protein turnover and possibly homeostasis.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1187274
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2010
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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