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Nucleic Acids Research Advance Access originally published online on December 20, 2007
Nucleic Acids Research 2008 36(4):1129-1137; doi:10.1093/nar/gkm1128
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Nucleic Acids Research, 2008, Vol. 36, No. 4 1129-1137
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea

Li Guo1, Yingang Feng2, Zhenfeng Zhang1, Hongwei Yao2, Yuanming Luo1, Jinfeng Wang2 and Li Huang1,*

1State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, 3A Datun Road, Beijing 100101, P. R. China and 2National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, P.R. China

*To whom correspondence should be addressed. Tel: +86 10 64807430; Fax: +86 10 64807429; Email: huangl{at}sun.im.ac.cn.

Correspondence may also be addressed to Jinfeng Wang. Tel: +86 10 64888490; Fax: +86 10 64872026; Email: jfw{at}sun5.ibp.ac.cn.

Received October 30, 2007. Revised December 3, 2007. Accepted December 4, 2007.

Archaea contain a variety of chromatin proteins consistent with the evolution of different genome packaging mechanisms. Among the two main kingdoms in the Archaea, Euryarchaeota synthesize histone homologs, whereas Crenarchaeota have not been shown to possess a chromatin protein conserved at the kingdom level. We report the identification of Cren7, a novel family of chromatin proteins highly conserved in the Crenarchaeota. A small, basic, methylated and abundant protein, Cren7 displays a higher affinity for double-stranded DNA than for single-stranded DNA, constrains negative DNA supercoils and is associated with genomic DNA in vivo. The solution structure and DNA-binding surface of Cren7 from the hyperthermophilic crenarchaeon Sulfolobus solfataricus were determined by NMR. The protein adopts an SH3-like fold. It interacts with duplex DNA through a β-sheet and a long flexible loop, presumably resulting in DNA distortions through intercalation of conserved hydrophobic residues into the DNA structure. These data suggest that the crenarchaeal kingdom in the Archaea shares a common strategy in chromatin organization.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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