Structural Basis for Dimerization in DNA Recognition by Ga14

Journal Article · Tue Jan 01 04:00:00 EST 2008 · Structure

DOI:https://doi.org/10.1016/j.str.2008.03.015· OSTI ID:959996

Hong, M; Fitzgerald, M; Harper, S; Luo, C; Speicher, D; Marmorstein, R

Gal4 is a Zn2Cys6 binuclear cluster containing transcription factor that binds DNA as a homodimer 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 bound to DNA as a dimer, the structure of the 'complete' Gal4 dimer bound to DNA has not previously been described. Here we report the structure of a complete Gal4 dimer bound to DNA and additional biochemical studies to address the molecular basis for Gal4 dimerization in DNA binding. We find that Gal4 dimerization on DNA is mediated by an intertwined helical bundle that deviates significantly from the solution NMR structure of the free dimerization domain. Associated biochemical studies show that the dimerization domain of Gal4 is important for DNA binding and protein thermostability. We also map the interaction surface of the Gal4 dimerization domain with Gal11P.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 959996
• Report Number(s): BNL--82982-2009-JA
• Journal Information: Structure, Journal Name: Structure Journal Issue: 7 Vol. 16
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
DIMERIZATION
DIMERS
DNA
MUTANTS
PROTEINS
TRANSCRIPTION
TRANSCRIPTION FACTORS
national synchrotron light source