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|2bky, resolution 1.70Å ()|
|Related:||1h0x, 1h0y, 1udv|
CRYSTAL STRUCTURE OF THE ALBA1:ALBA2 HETERODIMER FROM SULFOLOBUS SOLFATARICUS
Organisms growing at elevated temperatures face a particular challenge to maintain the integrity of their genetic material. All thermophilic and hyperthermophilic archaea encode one or more copies of the Alba (Sac10b) gene. Alba is an abundant, dimeric, highly basic protein that binds cooperatively and at high density to DNA. Sulfolobus solfataricus encodes a second copy of the Alba gene, and the Alba2 protein is expressed at approximately 5% of the level of Alba1. We demonstrate by NMR, ITC, and crystallography that Alba2 exists exclusively as a heterodimer with Alba1 at physiological concentrations and that heterodimerization exerts a clear effect upon the DNA packaging, as observed by EM, potentially by changing the interface between adjacent Alba dimers in DNA complexes. A functional role for Alba2 in modulation of higher order chromatin structure and DNA condensation is suggested.
Obligate heterodimerization of the archaeal Alba2 protein with Alba1 provides a mechanism for control of DNA packaging., Jelinska C, Conroy MJ, Craven CJ, Hounslow AM, Bullough PA, Waltho JP, Taylor GL, White MF, Structure. 2005 Jul;13(7):963-71. PMID:16004869
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
[ALBA1_SULSO] Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. May bind rRNA and mRNA, playing a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.[HAMAP-Rule:MF_01122] [ALBA2_SULSO] Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).