Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 409, Issue 2, Pages 341-348Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0003-9861(02)00639-2
Keywords
Saccharomyces cerevisiae; proteasome; 19S regulatory particle; N-acetylation; N-myristoylation; two-dimensional polyacrylamide gel; electrophoresis; mass spectrometry
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Funding
- NIGMS NIH HHS [R01 GM12702] Funding Source: Medline
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The yeast (Saccharomyces cerevisiae) contains three N-acetyltransferases, NatA, NatB, and NatC, each of which acetylates proteins with different N-terminal regions. The 19S regulatory particle of the yeast 26S proteasome consists of 17 subunits, 12 of which are N-terminally modified. By using nat1, nat3, and nat3 deletion mutants, we found that 8 subunits, Rpt4, Rpt5, Rpt6, Rpn2, Rpn3, Rpn5, Rpn6, and Rpn8, were NatA substrates, and that 2 subunits, Rpt3 and Rpn11, were NatB substrates. Mass spectrometric analysis revealed that the initiator Met of Rpt2 precursor polypeptide was processed and a part of the mature Rpt2 was N-myristoylated. The crude extracts from the normal strain and the nat1 deletion mutant were similar in chymotrypsin-like activity in the presence of ATP in vitro and in the accumulation level of the 26S proteasome. These characteristics were different from those of the 20S proteasome: the chymotrypsin-like activity and accumulation level of 20S proteasome were appreciably higher from the nat1 deletion mutant than from the normal strain. (C) 2002 Elsevier Science (USA). All rights reserved.
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