FEBS Letters
Volume 580, Issue 3 , Pages 717-719, 6 February 2006

Does the proteome encode organellar pH?

Edited by Takashi Gojobori

  • Christopher L. Brett

      Affiliations

    • Department of Physiology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA
    • Department of Medicine, The Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287, USA
    • Present address: School of Medicine, Department of Biochemistry, University of Washington, 1705 N.E. Pacific Street, Box 357350, Seattle, WA 98195, USA.
  • ,
  • Mark Donowitz

      Affiliations

    • Department of Physiology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA
    • Department of Medicine, The Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287, USA
  • ,
  • Rajini Rao

      Affiliations

    • Department of Physiology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA
    • Corresponding Author InformationCorresponding author.

Received 21 October 2005; received in revised form 27 December 2005; accepted 28 December 2005. published online 06 January 2006.

Abstract 

Inherent to the proteome itself, may be information that enables proteins to buffer pH at a level that promotes their own function within a specialized compartment. We observe that the distribution of computed isoelectric points in the yeast proteome matches experimentally derived organellar pH estimates across distinct subcellular compartments. This raises an interesting evolutionary question: did the pI of proteins and the pH of organelles co-evolve to optimize function?

Keywords: pI, pH, Proteome, Yeast, Subcellular compartment, Evolution

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PII: S0014-5793(06)00032-9

doi:10.1016/j.febslet.2005.12.103

FEBS Letters
Volume 580, Issue 3 , Pages 717-719, 6 February 2006