Structure of the full-length yeast Arp7-Arp9 heterodimer.
The nuclear actin-related proteins Arp7 and Arp9 are components of the yeast SWI/SNF and RSC chromatin-remodelling complexes. The 3.1 A resolution crystal structure reported here shows that the full-length Arp7 and Arp9 proteins exist as a dimer without a requirement for additional polypeptides. Of the 11 actin-related proteins, Arp7 and Arp9 ... are the only two directly demonstrated to form a dimer within this family. The Arp7-Arp9 heterodimer is unlikely to form an actin-like filament based on modelling using the structure. The Arp7-Arp9 structure reveals that its dimerization interface is not altered when bound in a complex with the SWI/SNF Snf2 HSA domain and the regulatory protein Rtt102.
Mesh Terms:
Amino Acid Sequence, Carrier Proteins, Chromosomal Proteins, Non-Histone, Crystallography, X-Ray, Escherichia coli, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Amino Acid Sequence, Carrier Proteins, Chromosomal Proteins, Non-Histone, Crystallography, X-Ray, Escherichia coli, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Acta Crystallogr. D Biol. Crystallogr.
Date: Feb. 01, 2014
PubMed ID: 24531465
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