Published online before print
April 11, 2001, 10.1101/gr.GR-1587R
Vol. 11, Issue 5, 703-709, May 2001
Whole Proteome pI Values Correlate with Subcellular Localizations of Proteins for Organisms within the Three Domains of Life
Russell
Schwartz,1,2,3,4
Claire S.
Ting,1,2 and
Jonathan
King1
1 Department of Biology, Massachusetts Institute of
Technology, Cambridge, Massachusetts 02139, USA
Isoelectric point (pI) values have long been a standard measure for
distinguishing between proteins. This article analyzes distributions of
pI values estimated computationally for all predicted ORFs in a
selection of fully sequenced genomes. Histograms of pI values confirm
the bimodality that has been observed previously for bacterial and
archaeal genomes (Van Bogelen et al. 1999) and reveal a trimodality in
eukaryotic genomes. A similar analysis on subsets of a nonredundant
protein sequence database generated from the full database by selecting
on subcellular localization shows that sequences annotated as
corresponding to cytosolic and integral membrane proteins have pI
distributions that appear to correspond with the two observed modes of
bacteria and archaea. Furthermore, nuclear proteins have a broader
distribution that may account for the third mode observed in
eukaryotes. On the basis of this association between pI and subcellular
localization, we conclude that the bimodal character of whole proteome
pI values in bacteria and archaea and the trimodal character in
eukaryotes are likely to be general properties of proteomes and are
associated with the need for different pI values depending on
subcellular localization. Our analyses also suggest that the
proportions of proteomes consisting of membrane-associated proteins may
be currently underestimated.
2
These authors contributed equally to this work.
3
Present address: Massachusetts Institute of Technology, 77 Massachusetts Avenue, Room 68-322, Cambridge, MA 02139, USA.
4
Corresponding author.
11:703-709 ©2001 by Cold Spring Harbor Laboratory Press ISSN 1088-9051/01 $5.00

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