RRC ID 52237
Author Miyamoto K, Uechi A, Saito K.
Title The zinc finger domain of RING finger protein 141 reveals a unique RING fold.
Journal Protein Sci.
Abstract Human RING finger protein 141 (RFP141) is a germ cell-specific transcription factor during spermatogenesis. We synthesized a compact construct encoding the C-terminal zinc finger of RFP141 (RFP141C peptide). Herein we determined the solution structure of the RFP141C peptide by nuclear magnetic resonance (NMR). Moreover, NMR data and the chemical modification of cysteine residues demonstrated that the RFP141C peptide binds to two zinc atoms in a cross-brace arrangement. The Simple Modular Architecture Research Tool database predicted the structure of RFP141C as a RING finger. However, the actual structure of the RFP141C peptide adopts an atypical compact C3 HC4 -type RING fold. The position and range of the helical active site of the RFP141C structure were elucidated at the atomic level. Therefore, structural analysis may allow RFP141C to be used for designing an artificial RING finger possessing specific ubiquitin-conjugating enzyme (E2)-binding capabilities.
Volume 26(8)
Pages 1681-1686
Published 2017-8
DOI 10.1002/pro.3201
PMID 28547869
PMC PMC5521587
MeSH Amino Acid Sequence Binding Sites Cations, Divalent DNA-Binding Proteins / chemistry* DNA-Binding Proteins / metabolism Humans Male Models, Molecular Nuclear Magnetic Resonance, Biomolecular Nuclear Proteins / chemistry* Nuclear Proteins / metabolism Peptides / chemical synthesis Peptides / chemistry* Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Domains Protein Folding* Protein Isoforms / chemistry Protein Isoforms / metabolism Sequence Alignment Sequence Homology, Amino Acid Spermatozoa / chemistry Spermatozoa / metabolism Thermodynamics Zinc / chemistry*
IF 2.42
Times Cited 3
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