N-terminal acetylation of cellular proteins creates specific degradation signals

Science

Volumn 327, Issue 5968, 2010, Pages 973-977

  Hwang, Cheol Sang ^a   Shemorry, Anna ^a   Varshavsky, Alexander ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CELL PROTEIN; CYSTEINE; METHIONINE; SERINE; THREONINE; UBIQUITIN PROTEIN LIGASE; VALINE;

BIOCHEMISTRY; DEGRADATION; ENZYME ACTIVITY; MICROBIAL ACTIVITY; PROTEIN; YEAST;

ACETYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN MODIFICATION; REGULATORY MECHANISM; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

ACETYLATION; ALANINE; AMINO ACID SEQUENCE; CYSTEINE; HALF-LIFE; METHIONINE; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SERINE; SUBSTRATE SPECIFICITY; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION; VALINE;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 77149120798     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1183147     Document Type: Article

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32. We thank J. Zhou (Caltech) for MS analyses and C. Brower for comments on the paper. We are grateful to members of the Varshavsky laboratory for their advice in the course of this study and particularly thank O. Batygin for her technical assistance. This work was supported by grants from NIH and the March of Dimes Foundation to A.V.