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Structure of the MalB Region in Escherichia Coli K12. I. Genetic Map of the MalK-lamB Operon

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Journal Mol Gen Genet
Date 1979 Jul 24
PMID 384166
Citations 57
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Abstract

A series of deletions, Mu insertions and point mutations affecting the malK-lamB operon have been isolated. They were used to establish a deletion map of this operon, which could be divided in 27 intervals, with 16 in malK and 11 in lamB. One interesting feature of this map is the lack of randomness in the distribution of Mu insertions in the lamB gene; by using data published elsewhere on the physical length of the deletion intervals it can be concluded that about 25% of these Mu insertions are clustered in a segment representing 2 to 8% of the gene. This map is presently being used to study the biosynthesis, structure, and function of the lamB product, which is an outer membrane protein involved in the transport of maltose and maltodextrin, and which in addition constitutes the receptor for phage lambda.

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References
1.
Schwartz M, Kellermann O, Szmelcman S, Hazelbauer G . Further studies on the binding of maltose to the maltose-binding protein of Escherichia coli. Eur J Biochem. 1976; 71(1):167-70. DOI: 10.1111/j.1432-1033.1976.tb11102.x. View

2.
Kellermann O, Szmelcman S . Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur J Biochem. 1974; 47(1):139-49. DOI: 10.1111/j.1432-1033.1974.tb03677.x. View

3.
Hazelbauer G . Role of the receptor for bacteriophage lambda in the functioning of the maltose chemoreceptor of Escherichia coli. J Bacteriol. 1975; 124(1):119-26. PMC: 235872. DOI: 10.1128/jb.124.1.119-126.1975. View

4.
Silhavy T, Shuman H, Beckwith J, Schwartz M . Use of gene fusions to study outer membrane protein localization in Escherichia coli. Proc Natl Acad Sci U S A. 1977; 74(12):5411-5. PMC: 431741. DOI: 10.1073/pnas.74.12.5411. View

5.
Raibaud O, CLEMENT J, Hofnung M . Structure of the malB region in Escherichia coli K12. III. Correlation of the genetic map with the restriction map. Mol Gen Genet. 1979; 174(3):261-7. DOI: 10.1007/BF00267798. View