Affordable Access

Mutations of the WD repeats that compromise Tup1 repression function maintain structural integrity of the WD domain trypsin-resistant core.

Authors
  • Zhang, Zhizhou
  • Varanasi, Usha
  • Carrico, Pauline
  • Trumbly, Robert J
Type
Published Article
Journal
Archives of biochemistry and biophysics
Publication Date
Oct 01, 2002
Volume
406
Issue
1
Pages
47–54
Identifiers
PMID: 12234489
Source
Medline
License
Unknown

Abstract

The yeast global transcriptional repressor Tup1 contains 7 WD repeats in its C-terminus that form a beta-propeller-like structure, in which the first and last WD repeats interact to make a closed circle. The WD domains of all proteins tested, including Tup1, form a compact structure resistant to trypsin digestion (Garcia-Higuera et al., Biochemistry 35 (1996) 13985-13994). We found that the in vitro formation of the trypsin-resistant core of Tup1 requires just five WD repeats (WD2-6). Deletion of the ST region between WD1 and WD2 destabilizes the trypsin-resistant core, but maintains Tup1 repression function in vivo. Linker insertion and point mutations in the WD repeats that compromise Tup1 repression function in vivo still maintain the trypsin-resistant core in vitro These results indicate that structural perturbation of the WD domain structure cannot explain the effects of these mutations on Tup1 repression function.

Report this publication

Statistics

Seen <100 times