Yeast UBL-UBA Proteins Have Partially Redundant Functions in Cell Cycle Control

Overview

Journal Cell Div

Publisher Biomed Central

Date 2006 Dec 6

PMID 17144915

Citations 31

Authors

Laura A Diaz-Martinez

Yang Kang

Kylie J Walters

Duncan J Clarke

Affiliations

Soon will be listed here.

Abstract

Background: Proteins containing ubiquitin-like (UBL) and ubiquitin associated (UBA) domains have been suggested to shuttle ubiquitinated substrates to the proteasome for degradation. There are three UBL-UBA containing proteins in budding yeast: Ddi1, Dsk2 and Rad23, which have been demonstrated to play regulatory roles in targeting ubiquitinated substrates to the proteasome for degradation. An involvement of these proteins in cell cycle related events has also been reported. We tested whether these three proteins act redundantly in the cell cycle.

Results: Here we show that the UBL-UBA proteins are partially redundant for cell cycle related roles. RAD23 is redundant with DDI1 and DSK2, but DDI1 and DSK2 are not redundant with each other and the triple deletion shows a synthetic effect, suggesting the existence of at least two roles for RAD23 in cell cycle control. The rad23Deltaddi1Deltadsk2Delta triple deletion strain delays both in G2/M-phase and in mid-anaphase at high temperatures with duplicated spindle pole bodies. Cell cycle progression in the triple deletion strain can only be partially rescued by a rad23 allele lacking the c-terminal UBA domain, suggesting that RAD23 requires its c-terminal UBA domain for full function. In addition to their ability to bind ubiquitin and the proteasome, the UBL-UBA proteins also share the ability to homodimerize. Rad23 and Dsk2 dimerization requires their UBL and/or UBA domains whereas Ddi1 dimerization does not. Here we show that Ddi1 homodimerization is necessary for its cell cycle related functions.

Conclusion: The three yeast UBL-UBA proteins have partially redundant roles required for progression through mitosis.

Citing Articles

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Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.

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