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Molecular and Cellular Biology, May 1999, p. 3466-3473, Vol. 19, No. 5
0270-7306/99/$04.00+0

Specific Acetylation of Chromosomal Protein HMG-17 by PCAF Alters Its Interaction with Nucleosomes

Julio E. Herrera,1,* Kazuyasu Sakaguchi,2 Michael Bergel,1 Lothar Trieschmann,1 Yoshihiro Nakatani,3 and Michael Bustin1

Protein Section, Laboratory of Molecular Carcinogenesis,1 and Chemistry Section, Laboratory of Cell Biology,2 Division of Basic Sciences, National Cancer Institute, and Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development,3 National Institutes of Health, Bethesda, Maryland 20892

Received 2 December 1998/Returned for modification 20 January 1999/Accepted 26 January 1999

Nonhistone chromosomal proteins HMG-14 and HMG-17 are closely related nucleosomal binding proteins that unfold the higher-order chromatin structure, thereby enhancing the transcription and replication potential of chromatin. Here we report that PCAF, a transcription coactivator with intrinsic histone acetyltransferase activity, specifically acetylates HMG-17 but not HMG-14. Using mass spectrum sequence analysis, we identified the lysine at position 2 as the predominant site acetylated by PCAF. Lysine 2 is a prominent acetylation site in vivo, suggesting that this PCAF-mediated acetylation is physiologically relevant. Experiments with HMG-17 deletion mutants and competition studies with various protein fragments indicate that the specific acetylation of HMG-17 is not determined solely by the primary sequence near the acetylation site. By equilibrium dialysis we demonstrated that acetylation reduces the affinity of HMG-17 to nucleosome cores. In addition, we found that the binding of HMG-14 and HMG-17 to nucleosome cores inhibits the PCAF-mediated acetylation of histone H3. Thus, the presence of HMG-14 and HMG-17 affects the ability of PCAF to acetylate chromatin, while the acetylation of HMG-17 reduces its binding affinity to chromatin. Conceivably, in HMG-17-containing chromatin, acetylation of HMG-17 precedes the acetylation of histones.

* Corresponding author. Mailing address: Bldg. 37, Rm. 3D-20, NIH, NCI, Bethesda, MD 20892. Phone: (301) 496-2885. Fax: (301) 496-8419. E-mail: Herr{at}helix.nih.gov.

Molecular and Cellular Biology, May 1999, p. 3466-3473, Vol. 19, No. 5
0270-7306/99/$04.00+0


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