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J. Biol. Chem., Vol. 267, Issue 4, 2329-2336, Feb, 1992
RE Kerppola and GF Ames
The membrane-bound complex of periplasmic permeases comprises two
hydrophobic proteins which have been hypothesized to be integral
membrane-spaninning proteins. We have investigated the topological
organization of the hydrophobic components of the Salmonella typhimurium
histidine permease, HisQ and HisM. Both proteins are digested by trypsin
and proteinase K when either inside-out or right- side-out membrane
vesicles are used. Therefore, these proteins are exposed to both surfaces
of the membrane. Digestion with carboxypeptidase and binding studies with
antibodies directed against the carboxyl terminus of HisQ and HisM have
localized their carboxyl termini to the inside surface of the cytoplasmic
membrane. Aminopeptidase digestion suggests periplasmic localization of
their amino termini. Alkaline phosphatase fusions to HisQ and HisM indicate
the existence of five spanners in both proteins. The periodicity and
orientation of spanners and loops in HisQ and HisM match those of the five
carboxyl-terminal spanners of MalF, the only other hydrophobic component of
the periplasmic permeases for which topological information is available.
An alignment of the sequences of all known hydrophobic components of
periplasmic permeases is presented which indicates clear conservation of
secondary structure and some conservation of primary sequence. The
structural conservation of the components is discussed, and a role for a
hydrophilic loop containing a conserved sequence (the EAA loop) is
proposed.
Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family
Department of Molecular and Cellular Biology, University of California, Berkeley 94720.
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