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EMBO J. 1986 Nov;5(11):3021-7.

The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology.

Author information

1
Research Group for Theoretical Biophysics, Department of Theoretical Physics, Royal Institute of Technology, S-100 44 Stockholm, Sweden.

Abstract

The amino acid distribution in membrane spanning segments and connecting loops in bacterial inner membrane proteins was analysed. The basic residues Arg and Lys are four times less prevalent in periplasmic as compared to cytosolic connecting loops, whereas no comparable effect is observed for the acidic residues Asp and Glu. Also, Pro is shown to be tolerated to a much larger extent in membrane spanning segments with their N-terminus pointing towards the cytosol than in those with the opposite orientation. The significance of these findings with regard to the mechanism of biogenesis of bacterial inner membrane proteins is discussed.

PMID:
16453726
PMCID:
PMC1167256

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