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 language | English (US) |
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Pages (from-to) | 677-687 |
Number of pages | 11 |
Journal | Biochimica et Biophysica Acta - Gene Regulatory Mechanisms |
Volume | 1849 |
Issue number | 6 |
DOIs | |
State | Published - 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