Universität zu Köln

Marshall, Richard S., Gemperline, David C., McLoughlin, Fionn, Book, Adam J., Hofmann, Kay ORCID: 0000-0002-2289-9083 and Vierstra, Richard D. (2020). An evolutionarily distinct chaperone promotes 20S proteasome alpha-ring assembly in plants. J. Cell Sci., 133 (21). CAMBRIDGE: COMPANY BIOLOGISTS LTD. ISSN 1477-9137

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Abstract

The core protease (CP) subcomplex of the 26S proteasome houses the proteolytic active sites and assumes a barrel shape comprised of four co-axially stacked heptameric rings formed by structurally related alpha- and beta-subunits. CP biogenesis typically begins with the assembly of the alpha-ring, which then provides a template for beta-subunit integration. In eukaryotes, alpha-ring assembly is partially mediated by two heterodimeric chaperones, termed Pba1-Pba2 (Add66) and Pba3-Pba4 (also known as Irc25-Poc4) in yeast. Pba1-Pba2 initially promotes orderly recruitment of the alpha-subunits through interactions between their C-terminal HbYX or HbF motifs and pockets at the alpha(5)-alpha(6) and alpha(6)-alpha(7) interfaces. Here, we identified PBAC5 as a fifth alpha-ring assembly chaperone in Arabidopsis that directly binds the Pba1 homolog PBAC1 to form a trimeric PBAC5-PBAC1-PBAC2 complex. PBAC5 harbors a HbYX motif that docks with a pocket between the alpha(4) and alpha(5) subunits during alpha-ring construction. Arabidopsis lacking PBAC5, PBAC1 and/or PBAC2 are hypersensitive to proteotoxic, salt and osmotic stresses, and display proteasome assembly defects. Remarkably, whereas PBAC5 is evolutionarily conserved among plants, sequence relatives are also dispersed within other kingdoms, including a scattered array of fungal, metazoan and oomycete species.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Marshall, Richard S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Gemperline, David C. UNSPECIFIED UNSPECIFIED UNSPECIFIED McLoughlin, Fionn UNSPECIFIED UNSPECIFIED UNSPECIFIED Book, Adam J. UNSPECIFIED UNSPECIFIED UNSPECIFIED Hofmann, Kay UNSPECIFIED orcid.org/0000-0002-2289-9083 UNSPECIFIED Vierstra, Richard D. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-312658
DOI:	10.1242/jcs.249862
Journal or Publication Title:	J. Cell Sci.
Volume:	133
Number:	21
Date:	2020
Publisher:	COMPANY BIOLOGISTS LTD
Place of Publication:	CAMBRIDGE
ISSN:	1477-9137
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language PROTEIN-QUALITY CONTROL; 26S PROTEASOME; CORE PARTICLE; S PROTEASOME; SUBUNIT; COMPLEX; YEAST; IDENTIFICATION; PURIFICATION; DEGRADATION Multiple languages Cell Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/31265