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The destruction box of the cyclin Clb2 binds the anaphase-promoting complex/cyclosome subunit Cdc23.

Abstract：

:Properly regulated cyclin proteolysis is critical for normal cell cycle progression. A nine-amino acid peptide motif called the destruction box (D box) is present at the N terminus of the yeast mitotic cyclins. This short sequence is required for cyclin ubiquitination and subsequent proteolysis. The anaphase-promoting complex/cyclosome (APC/C) is a multisubunit E3 required for cyclin ubiquitination. We have tested the D box of five mitotic cyclins for interaction with six APC/C subunits. The APC/C subunit Cdc23, but not five other subunits tested, interacted by two-hybrid analysis with the N terminus of wild-type Clb2. None of these subunits interacted with the N termini of the cyclins Clb1, Clb3, or Clb5. Mutations in the D box sequences of Clb2 inhibited interaction with Cdc23 both in vivo and in vitro. Our results provide the first evidence for a direct interaction between an APC/C substrate (Clb2) and an APC/C subunit (Cdc23).

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Meyn MA 3rd,Melloy PG,Li J,Holloway SL

doi

10.1016/s0003-9861(02)00467-8

subject

Has Abstract

pub_date

2002-11-15 00:00:00

pages

189-95

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003986102004678

journal_volume

407

pub_type

杂志文章

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