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An asymmetric interface between the regulatory and core particles of the proteasome.

Abstract：

:The Saccharomyces cerevisiae proteasome comprises a 19-subunit regulatory particle and a 28-subunit core particle. To be degraded, substrates must cross the core particle-regulatory particle interface, a site for complex conformational changes and regulatory events. This interface includes two aligned heteromeric rings, one formed by the six ATPase (Rpt) subunits of the regulatory particle and the other by the seven α subunits of the core particle. The Rpt C termini bind to intersubunit cavities in the α-ring, thus directing core particle gating and proteasome assembly. We mapped the Rpt C termini to the α subunit pockets, using a cross-linking approach that revealed an unexpected asymmetry: one side of the ring shows 1:1 contacts of Rpt2-α4, Rpt6-α3 and Rpt3-α2, whereas on the opposite side, the Rpt1, Rpt4 and Rpt5 tails each cross-link to multiple α pockets. Rpt-core particle cross-links are all sensitive to nucleotides, implying that ATP hydrolysis drives dynamic alterations at the core particle-regulatory particle interface.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Tian G,Park S,Lee MJ,Huck B,McAllister F,Hill CP,Gygi SP,Finley D

doi

10.1038/nsmb.2147

subject

Has Abstract

pub_date

2011-10-30 00:00:00

pages

1259-67

issue

11

eissn

1545-9993

issn

1545-9985

pii

nsmb.2147

journal_volume

18

pub_type

杂志文章

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