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Molecular and Cellular Biology, August 2009, p. 4220-4234, Vol. 29, No. 15
0270-7306/09/$08.00+0     doi:10.1128/MCB.01882-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

An Rtt109-Independent Role for Vps75 in Transcription-Associated Nucleosome Dynamics{triangledown} ,{dagger}

Luke A. Selth,1 Yahli Lorch,2 Maria T. Ocampo-Hafalla,3 Richard Mitter,4 Michael Shales,5 Nevan J. Krogan,5 Roger D. Kornberg,2 and Jesper Q. Svejstrup1*

Clare Hall Laboratories, Cancer Research UK London Research Institute, Blanche Lane, South Mimms, Hertfordshire EN6 3LD, United Kingdom,1 Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305,2 Chromosome Segregation Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London, United Kingdom,3 Bioinformatics, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London, United Kingdom,4 Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 941585

Received 11 December 2008/ Returned for modification 12 February 2009/ Accepted 15 May 2009

The histone chaperone Vps75 forms a complex with, and stimulates the activity of, the histone acetyltransferase Rtt109. However, Vps75 can also be isolated on its own and might therefore possess Rtt109-independent functions. Analysis of epistatic miniarray profiles showed that VPS75 genetically interacts with factors involved in transcription regulation whereas RTT109 clusters with genes linked to DNA replication/repair. Additional genetic and biochemical experiments revealed a close relationship between Vps75 and RNA polymerase II. Furthermore, Vps75 is recruited to activated genes in an Rtt109-independent manner, and its genome-wide association with genes correlates with transcription rate. Expression microarray analysis identified a number of genes whose normal expression depends on VPS75. Interestingly, histone H2B dynamics at some of these genes are consistent with a role for Vps75 in histone H2A/H2B eviction/deposition during transcription. Indeed, reconstitution of nucleosome disassembly using the ATP-dependent chromatin remodeler Rsc and Vps75 revealed that these proteins can cooperate to remove H2A/H2B dimers from nucleosomes. These results indicate a role for Vps75 in nucleosome dynamics during transcription, and importantly, this function appears to be largely independent of Rtt109.

* Corresponding author. Mailing address: Clare Hall Laboratories, Cancer Research UK London Research Institute, Blanche Lane, South Mimms, Hertfordshire EN6 3LD, United Kingdom. Phone: 44 (0)1707 625960. Fax: 44 (0)1707 625801. E-mail: j.svejstrup{at}cancer.org.uk

{triangledown} Published ahead of print on 26 May 2009.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, August 2009, p. 4220-4234, Vol. 29, No. 15
0270-7306/09/$08.00+0     doi:10.1128/MCB.01882-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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