Zn-binding motifs, ubiquitous among gene-regulatory factors, provide an economical mechanism of metal-dependent protein folding. In earlier studies we described a novel Zn-binding motif in the nucleic-acid binding domain of human transcriptional elongation factor TFIIS. The NMR structure consists of a three-stranded antiparallel ?-sheet designated the Zn ribbon. Analysis of the sequence database suggested a conserved family of Zn-ribbon motifs in a diverse family of nucleic-acid-binding proteins, including RNA polymerase itself. The intriguing discovery of a putative Zn ribbon sequence in an archeal genome (Kaine, B.P., Mehr, I.J., & Woese, C.R. (1994) Proc. Natl. Acad. Sci. USA 91, 3854-8) now permits this hypothesis to be tested directed in a system of exception thermal stability. The archeal gene encodes a protein homologous to a subunit of human RNA polymerase II. We propose to determine the solution structure of this RNA polymerase subunit by multidimensional heteronuclear NMR methods.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR002301-16
Application #
6309184
Study Section
Project Start
2000-04-15
Project End
2005-02-28
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
16
Fiscal Year
2000
Total Cost
$7,533
Indirect Cost
Name
University of Wisconsin Madison
Department
Type
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
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