Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Solution structure of the n-terminal zinc fingers of the xenopus laevis double-stranded rna-binding protein zfa

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Moller, H. M.
  • Martinez-Yamout, M. A.
  • Dyson, Jane
  • Wright, Peter

publication date

  • August 2005

journal

  • Journal of Molecular Biology  Journal

abstract

  • Several zinc finger proteins have been discovered recently that bind specifically to double-stranded RNA. These include the mammalian JAZ and wig proteins, and the seven-zinc finger protein ZFa from Xenopus laevis. We have determined the solution structure of a 127 residue fragment of ZFa, which consists of two zinc finger domains connected by a linker that remains unstructured in the free protein in solution. The first zinc finger consists of a three-stranded beta-sheet and three helices, while the second finger contains only a two-stranded sheet and two helices. The common structures of the core regions of the two fingers are superimposable. Each finger has a highly electropositive surface that maps to a helix-kink-helix motif. There is no evidence for interactions between the two fingers, consistent with the length (24 residues) and unstructured nature of the intervening linker. Comparison with a number of other proteins shows similarities in the topology and arrangement of secondary structure elements with canonical DNA-binding zinc fingers, with protein interaction motifs such as FOG zinc fingers, and with other DNA-binding and RNA-binding proteins that do not contain zinc. However, in none of these cases does the alignment of these structures with the ZFa zinc fingers produce a consistent picture of a plausible RNA-binding interface. We conclude that the ZFa zinc fingers represent a new motif for the binding of double-stranded RNA.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cell Cycle Proteins
  • Circular Dichroism
  • Fungal Proteins
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • RNA, Double-Stranded
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
  • Solutions
  • Static Electricity
  • Transcription Factor TFIIIA
  • Transcription Factors
  • Xenopus Proteins
  • Xenopus laevis
  • Zinc Fingers
scroll to property group menus

Research

keywords

  • JAZ
  • NMR
  • helix-loop-helix
  • helix-turn-helix
  • wig-1
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2005.06.032

PubMed ID

  • 16051273
scroll to property group menus

Additional Document Info

start page

  • 718

end page

  • 730

volume

  • 351

issue

  • 4

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support