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Regulation of high-affinity leucine transport in Escherichia coli.

Authors :
Landick R
Anderson JJ
Mayo MM
Gunsalus RP
Mavromara P
Daniels CJ
Oxender DL
Source :
Journal of supramolecular structure [J Supramol Struct] 1980; Vol. 14 (4), pp. 527-37.
Publication Year :
1980

Abstract

Leucine is transported into E coli by two osmotic shock-sensitive, high-affinity systems (LIV-I and leucine-specific systems) and one membrane bound, low-affinity system (LIV-II). Expression of the high-affinity transport systems is altered by mutations in livR and 1stR, genes for negatively acting regulatory elements, and by mutations in rho, the gene for transcription termination. All four genes for high-affinity leucine transport (livJ, livK, livH, and livG) are closely linked and have been cloned on a plasmid vector, pOX1. Several subcloned fragments of this plasmid have been prepared and used in complementation and regulation studies. The results of these studies suggest that livJ and livK are separated by approximately one kilobase and give a gene order of livJ-livK-livH. livJ and livK appear to be regulated in an interdependent fashion; livK is expressed maximally when the livJ gene is activated by mutation or deletion. The results support the existence of separate promotors for the livJ and livK genes. The effects of mutations in the rho and livR genes are additive on one another and therefore appear to be involved in independent regulatory mechanisms. Mutations in the rho gene affect both the LIV-I and leucine-specific transport systems by increasing the expression of livJ and livK, genes for the LIV-specific and leucine-specific binding proteins, respectively.

Details

Language :
English
ISSN :
0091-7419
Volume :
14
Issue :
4
Database :
MEDLINE
Journal :
Journal of supramolecular structure
Publication Type :
Academic Journal
Accession number :
7017282
Full Text :
https://doi.org/10.1002/jss.400140410