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Title: Insights into Strand Exchange in BTB Domain Dimers from the Crystal Structures of FAZF and Miz1

Abstract

The BTB domain is a widely distributed protein-protein interaction motif that is often found at the N-terminus of zinc finger transcription factors. Previous crystal structures of BTB domains have revealed tightly interwound homodimers, with the N-terminus from one chain forming a two-stranded anti-parallel {beta}-sheet with a strand from the other chain. We have solved the crystal structures of the BTB domains from Fanconi anemia zinc finger (FAZF) and Miz1 (Myc-interacting zinc finger 1) to resolutions of 2.0 {angstrom} and 2.6 {angstrom}, respectively. Unlike previous examples of BTB domain structures, the FAZF BTB domain is a nonswapped dimer, with each N-terminal {beta}-strand associated with its own chain. As a result, the dimerization interface in the FAZF BTB domain is about half as large as in the domain-swapped dimers. The Miz1 BTB domain resembles a typical swapped BTB dimer, although it has a shorter N-terminus that is not able to form the interchain sheet. Using cysteine cross-linking, we confirmed that the promyelocytic leukemia zinc finger (PLZF) BTB dimer is strand exchanged in solution, while the FAZF BTB dimer is not. A phylogenic tree of the BTB fold based on both sequence and structural features shows that the common ancestor of the BTBmore » domain in BTB-ZF (bric a brac, tramtrack, broad-complex zinc finger) proteins was a domain-swapped dimer. The differences in the N-termini seen in the FAZF and Miz1 BTB domains appear to be more recent developments in the structural evolution of the domain.« less

Authors:
; ; ; ;  [1];  [2]
  1. (Toronto)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002720
Resource Type:
Journal Article
Journal Name:
J. Mol. Biol.
Additional Journal Information:
Journal Volume: 400; Journal Issue: (5) ; 07, 2010; Journal ID: ISSN 0022-2836
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; ANEMIAS; CHAINS; CRYSTAL STRUCTURE; CYSTEINE; DIMERIZATION; DIMERS; DOMAIN STRUCTURE; LEUKEMIA; PROTEINS; TRANSCRIPTION FACTORS; ZINC

Citation Formats

Stogios, Peter J., Cuesta-Seijo, Jose Antonio, Chen, Lu, Pomroy, Neil C., Privé, Gilbert G., and OCI). Insights into Strand Exchange in BTB Domain Dimers from the Crystal Structures of FAZF and Miz1. United States: N. p., 2010. Web. doi:10.1016/j.jmb.2010.05.028.
Stogios, Peter J., Cuesta-Seijo, Jose Antonio, Chen, Lu, Pomroy, Neil C., Privé, Gilbert G., & OCI). Insights into Strand Exchange in BTB Domain Dimers from the Crystal Structures of FAZF and Miz1. United States. doi:10.1016/j.jmb.2010.05.028.
Stogios, Peter J., Cuesta-Seijo, Jose Antonio, Chen, Lu, Pomroy, Neil C., Privé, Gilbert G., and OCI). Wed . "Insights into Strand Exchange in BTB Domain Dimers from the Crystal Structures of FAZF and Miz1". United States. doi:10.1016/j.jmb.2010.05.028.
@article{osti_1002720,
title = {Insights into Strand Exchange in BTB Domain Dimers from the Crystal Structures of FAZF and Miz1},
author = {Stogios, Peter J. and Cuesta-Seijo, Jose Antonio and Chen, Lu and Pomroy, Neil C. and Privé, Gilbert G. and OCI)},
abstractNote = {The BTB domain is a widely distributed protein-protein interaction motif that is often found at the N-terminus of zinc finger transcription factors. Previous crystal structures of BTB domains have revealed tightly interwound homodimers, with the N-terminus from one chain forming a two-stranded anti-parallel {beta}-sheet with a strand from the other chain. We have solved the crystal structures of the BTB domains from Fanconi anemia zinc finger (FAZF) and Miz1 (Myc-interacting zinc finger 1) to resolutions of 2.0 {angstrom} and 2.6 {angstrom}, respectively. Unlike previous examples of BTB domain structures, the FAZF BTB domain is a nonswapped dimer, with each N-terminal {beta}-strand associated with its own chain. As a result, the dimerization interface in the FAZF BTB domain is about half as large as in the domain-swapped dimers. The Miz1 BTB domain resembles a typical swapped BTB dimer, although it has a shorter N-terminus that is not able to form the interchain sheet. Using cysteine cross-linking, we confirmed that the promyelocytic leukemia zinc finger (PLZF) BTB dimer is strand exchanged in solution, while the FAZF BTB dimer is not. A phylogenic tree of the BTB fold based on both sequence and structural features shows that the common ancestor of the BTB domain in BTB-ZF (bric a brac, tramtrack, broad-complex zinc finger) proteins was a domain-swapped dimer. The differences in the N-termini seen in the FAZF and Miz1 BTB domains appear to be more recent developments in the structural evolution of the domain.},
doi = {10.1016/j.jmb.2010.05.028},
journal = {J. Mol. Biol.},
issn = {0022-2836},
number = (5) ; 07, 2010,
volume = 400,
place = {United States},
year = {2010},
month = {9}
}