Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome

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4 Scopus citations

Abstract

The high-mobility group (HMG) domain containing proteins regulate transcription, DNA replication and recombination. They adopt L-shaped folds and are structure-specific DNA binding motifs. Here, I define the L-motif super-family that consists of DNA-binding HMG-box proteins and the L-motif of the histone mRNA binding domain of stem-loop binding protein (SLBP). The SLBP L-motif and HMG-box domains adopt similar L-shaped folds with three α-helices and two or three small hydrophobic cores that stabilize the overall fold, but have very different and distinct modes of nucleic acid recognition. A comparison of the structure, dynamics, protein-protein and nucleic acid interactions, and regulation by PTMs of the SLBP and the HMG-box L-motifs reveals the versatile and diverse modes by which L-motifs utilize their surfaces for structure-specific recognition of nucleic acids to regulate gene expression.

Original languageEnglish (US)
Pages (from-to)677-687
Number of pages11
JournalBiochimica et Biophysica Acta - Gene Regulatory Mechanisms
Volume1849
Issue number6
DOIs
StatePublished - May 15 2015

Keywords

  • DNA binding domain
  • HMG-box domain
  • Phosphorylation
  • Protein-nucleic acid interaction
  • RNA binding domain
  • Stem-loop binding protein (SLBP)

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics

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