Molecular evolution of NASP and conserved histone H3/H4 transport pathway
Open Access
- 20 June 2014
- journal article
- research article
- Published by Springer Nature in BMC Ecology and Evolution
- Vol. 14 (1) , 139
Abstract
NASP is an essential protein in mammals that functions in histone transport pathways and maintenance of a soluble reservoir of histones H3/H4. NASP has been studied exclusively in Opisthokonta lineages where some functional diversity has been reported. In humans, growing evidence implicates NASP miss-regulation in the development of a variety of cancers. Although a comprehensive phylogenetic analysis is lacking, NASP-family proteins that possess four TPR motifs are thought to be widely distributed across eukaryotes.Keywords
All Related Versions
This publication has 118 references indexed in Scilit:
- Codanin‐1, mutated in the anaemic disease CDAI, regulates Asf1 function in S‐phase histone supplyThe EMBO Journal, 2012
- A Specific Function for the Histone Chaperone NASP to Fine-Tune a Reservoir of Soluble H3-H4 in the Histone Supply ChainMolecular Cell, 2011
- The program for processing newly synthesized histones H3.1 and H4Nature Structural & Molecular Biology, 2010
- I-TASSER: a unified platform for automated protein structure and function predictionNature Protocols, 2010
- Protein structure prediction on the Web: a case study using the Phyre serverNature Protocols, 2009
- A NASP (N1/N2)-Related Protein, Sim3, Binds CENP-A and Is Required for Its Deposition at Fission Yeast CentromeresMolecular Cell, 2007
- Structure of a human ASF1a–HIRA complex and insights into specificity of histone chaperone complex assemblyNature Structural & Molecular Biology, 2006
- Tunicates and not cephalochordates are the closest living relatives of vertebratesNature, 2006
- From 2R to 3R: evidence for a fish‐specific genome duplication (FSGD)BioEssays, 2005
- Evolution by gene duplication: an updateTrends in Ecology & Evolution, 2003