Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a

Journal Article · Fri Oct 28 04:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.08.179· OSTI ID:20713403

Miranda, Tina Branscombe ^[1]; Webb, Kristofor J ^[1]; Edberg, Dale D ^[2]; Reeves, Raymond ^[3]; Clarke, Steven ^[1]

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1. Department of Chemistry and Biochemistry, Molecular Biology Institute, UCLA, Los Angeles, CA 90095-1560 (United States)
2. School of Molecular Biosciences, Washington State University, Pullman, Washington 99164 (United States)
3. The School of Molecular Biosciences, Washington State University, Pullman, Washington 99164 (United States)

The HMGA family proteins HMGA1a and HMGA1b are nuclear nonhistone species implicated in a wide range of cellular processes including inducible gene transcription, modulation of chromosome structure through nucleosome and chromosome remodeling, and neoplastic transformation. HMGA proteins are highly modified, and changes in their phosphorylation states have been correlated with the phase of the cell cycle and changes in their transcriptional activity. HMGA1a is also methylated in the first DNA-binding AT-hook at Arg25 and other sites, although the enzyme or enzymes responsible have not been identified. We demonstrate here that a GST fusion of protein arginine methyltransferase 6 (PRMT6) specifically methylates full-length recombinant HMGA1a protein in vitro. Although GST fusions of PRMT1 and PRMT3 were also capable of methylating the full-length HMGA1a polypeptide, they recognize its proteolytic degradation products much better. GST fusions of PRMT4 or PRMT7 were unable to methylate the full-length protein or its degradation products. We conclude that PRMT6 is a good candidate for the endogenous enzyme responsible for HGMA1a methylation.

• OSTI ID: 20713403
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 3 Vol. 336; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ARGININE
CELL CYCLE
CHROMATIN
CHROMOSOMES
DNA
ENZYMES
GENES
IN VITRO
METHYLATION
PHOSPHORYLATION
POLYPEPTIDES
TRANSCRIPTION