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

Article Details

Citation

Heijne G

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

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

PubMed ID
16453726 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Signal peptidase IP00803Details
Lactose permeaseP02920Details