Nucleic Acids Research Advance Access originally published online on September 18, 2006
Nucleic Acids Research 2006 34(17):4893-4899; doi:10.1093/nar/gkl434
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Nucleic Acids Research, 2006, Vol. 34, No. 17 4893-4899
© 2006 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.
Molecular Biology |
Identification of a structural and functional domain in xNAP1 involved in protein–protein interactions
Institute of Biomedical and Biomolecular Sciences, University of Portsmouth Portsmouth PO1 2DT, UK
*To whom correspondence should be addressed. Tel: 0044 2392 842678; Fax: 0044 2392 842053; Email: Geoff.Kneale{at}port.ac.uk
Received March 13, 2006. Revised May 18, 2006. Accepted June 1, 2006.
xNAP1 (Xenopus nucleosome assembly protein) belongs to the family of nucleosome assembly proteins (NAPs) and shares 92% identity with human and mouse NAP1. NAPs have been reported to have a role in nucleosome assembly, cell cycle regulation, cell proliferation and transcriptional control, although the precise function of NAP1 is still not clear. Here we report the identification of a putative domain of xNAP1 by limited proteolysis. This domain has been mapped in the xNAP1 protein sequence to residues 38–282 and thus lacks the acidic sequences at the N- and C-termini. We have studied this domain and related fragments in vitro and by a functional assay involving over-expression of the protein in Xenopus laevis embryos. Analytical ultracentrifugation shows that removal of the acidic N- and C-terminal regions does not prevent the formation of larger multimers, which are predominantly hexadecamers. Injection of mRNA encoding the full-length xNAP1 or the putative domain and other related constructs into Xenopus embryos gave identical phenotypes. These results are discussed in relation to protein–protein interactions between NAP1 octamers and a possible ‘squelching’ mechanism.
Present addresses: John McGeeghan, EMBL-Grenoble, Grenoble Cedex 9, France
Anita Abu-daya, NIMR, The Ridgeway, Mill Hill, London NW7 1AA, UK
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