Beta-galactoside transport in E. coli: a functional dissection of lac permease

H R Kaback; E Bibi; P D Roepe

doi:10.1016/0968-0004(90)90020-c

Beta-galactoside transport in E. coli: a functional dissection of lac permease

Trends Biochem Sci. 1990 Aug;15(8):309-14. doi: 10.1016/0968-0004(90)90020-c.

Authors

H R Kaback¹, E Bibi, P D Roepe

Affiliation

¹ Howard Hughes Medical Institute, Molecular Biology Institute, Los Angeles, CA 90024-1570.

PMID: 2204157
DOI: 10.1016/0968-0004(90)90020-c

Abstract

The polytopic membrane protein lac permease harnesses energy from the electrochemical H+ gradient to transport beta-galactosidases against a concentration gradient. Although high-resolution structural information is still lacking, the permease is thought to possess 12 membrane-spanning alpha-helical segments. Various experimental strategies, including site-directed mutagenesis, have been employed to probe the function of this membrane protein at the molecular level.

Publication types

Review

MeSH terms

Amino Acid Sequence
Biological Transport
Escherichia coli / enzymology*
Escherichia coli / metabolism
Escherichia coli Proteins*
Galactosides / metabolism*
Glycosides / metabolism*
Membrane Transport Proteins / physiology*
Molecular Sequence Data
Monosaccharide Transport Proteins*
Symporters*

Substances

Escherichia coli Proteins
Galactosides
Glycosides
LacY protein, E coli
Membrane Transport Proteins
Monosaccharide Transport Proteins
Symporters
beta-galactoside
lactose permease