A zinc-Cys6 binuclear cluster motif containing transcription factor: Structural and functional studies of the dimerization domain of Gal4.

Format:

Book

Thesis/Dissertation

Author/Creator:

Hong, Manqing.

Contributor:

University of Pennsylvania.

Language:

English

Subjects (All):

Biochemistry.

0487.

Local Subjects:

0487.

Physical Description:

140 pages

Contained In:

Dissertation Abstracts International 70-01B.

System Details:

Mode of access: World Wide Web.

text file

Summary:

Gal4 is the prototype of a family of proteins that contain the Zn 2Cys6 binuclear cluster DNA-binding motif and binds as a homodimer to DNA targets containing two inverted CGG half-sites. In addition, Gal4 is a transcription factor that regulates gene expression of enzymes involved in galactose metabolism by binding to their upstream activating sequence and can activate transcription by interacting with the mutant Gal11P protein. Although structures have been reported of the Gal4 dimerization domain and the binuclear cluster domain monomer bound to DNA as a dimer, the structure of the "complete" Gal4 dimer bound to DNA has not previously been described. This study presents the structure of a complete Gal4 dimer bound to DNA and related biochemical studies to address the molecular basis for Gal4 dimerization in DNA binding. Our studies show that Gal4 dimerization on DNA is mediated by an intertwined helical bundle that deviates significantly from the NMR structure of the free dimerization domain in the absence of DNA and that the Gal4 dimerization domain is important for DNA binding and protein thermostability. In addition, the interaction surface of the Gal4 dimerization domain with Gal11P was also mapped on the crystal structure.

Notes:

Source: Dissertation Abstracts International, Volume: 70-01, Section: B, page: 0269.

Adviser: Ronen Marmorstein.

Thesis (Ph.D.)--University of Pennsylvania, 2008.

Local Notes:

School code: 0175.

ISBN:

9781109008029

Access Restriction:

Restricted for use by site license.