A role for TBP dimerization in preventing unregulated gene expression.

Abstract:

:The recruitment of the TATA box-binding protein (TBP) to promoters in vivo is often rate limiting in gene expression. We present evidence that TBP negatively autoregulates its accessibility to promoter DNA in yeast through dimerization. The crystal structure of TBP dimers was used to design point mutations in the dimer interface. These mutants are impaired for dimerization in vitro, and in vivo they generate large increases in activator-independent gene expression. Overexpression of wild-type TBP suppresses these mutants, possibly by heterodimerizing with them. In addition to loss of autorepression, dimerization-defective TBPs are rapidly degraded in vivo. Direct detection of TBP dimers in vivo was achieved through chemical cross-linking. Taken together, the data suggest that TBP dimerization prevents unregulated gene expression and its own degradation.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Jackson-Fisher AJ,Chitikila C,Mitra M,Pugh BF

doi

10.1016/s1097-2765(01)80004-6

subject

Has Abstract

pub_date

1999-06-01 00:00:00

pages

717-27

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)80004-6

journal_volume

3

pub_type

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