Journal of
Biophysics and Structural Biology

  • Abbreviation: J. Biophys. Struct. Biol.
  • Language: English
  • ISSN: 2141-2200
  • DOI: 10.5897/JBSB
  • Start Year: 2009
  • Published Articles: 22

Full Length Research Paper

pH uniquely modulates protein arginine methylation

Wen Xie1, George Merz2 and Robert B. Denman3*
1Division of Hematology and Medical Oncology, Department of Medicine, Weill Medical College of Cornell University, New York, NY 10065, USA. 2Department of Developmental Neurobiology, New York State Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, NY 10314, USA. 3Department of Molecular Biology, New York State Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, NY 10314, USA.
Email: [email protected]

  •  Accepted: 02 August 2011
  •  Published: 30 November 2011

Abstract

Protein arginine methyltransferases (PRMTs) function in the alkaline milieu of the nucleus and at neutral pH of the cytosol. Accordingly, several PRMTs are broadly active over a range of pHs. We investigated the effect altering pH had on protein arginine methylation using a variety of defined substrates, recombinant PRMTs and cell extracts.We demonstrate that pH-induced alterations in the extent of methylation and the methyl-product formed depend both on the particular substrate assayed and the PRMT that modifies it. We also find that transient intracellular alkalinization of mouse embryonic P19 neurons by NH4Cl results in sustained changes in substrate methylation.  Altogether our results are consistent with a hypothesis in which altered substrate methylation resulting from pH-induced changes of PRMT activities coupled with low levels of demethylation may provide the long-term tag(s) necessary for the formation and maintenance of “molecular memory”.

 

Key words: Arginine methylation, protein arginine methyltransferase, pH, P19 cells, insect cell lysate, SmD1 peptide.

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