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Inactivation of the lactose permease of Escherichia coli by monochromatic ultraviolet light

Journal Article:

Abstract

The lactose permease of E. coli was inactivated exponetially by seven wavelengths of monochromatic UV light. An action spectrum revealed that the shorter wavelengths (243, 290 and 313 nm) were much more efficient than longer wavelengths. Inactivation at 290 nm was most efficient and was not due to generalized membrane damage. The rate of counterflux of intracellular ..beta..-galactoside in response to externally added ..beta..-galactoside was slowed by 290 nm irradiation, indicating destruction of the facilitated diffusion mechanism. The induction of ..beta..-galactosidase and ..beta..-galactoside permease was co-ordinate both with and without pre-irradiation by 290 nm light. The ..beta.. galactosidase was approximately 26-fold more resistant to 290 nm than the permease. These results are discussed in terms of a greater sensitivity of membrane proteins to 290 nm light, which may be due to the role of aromatic amino acids in conferring stability to the permease in the membrane.
Authors:
Robb, F T; Peak, M J [1] 
  1. Rhodes Univ., Grahamstown (South Africa)
Publication Date:
Sep 01, 1979
Product Type:
Journal Article
Reference Number:
AIX-11-502313; EDB-80-124836
Resource Relation:
Journal Name: Photochem. Photobiol.; (United Kingdom); Journal Volume: 3
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CELL MEMBRANES; RADIOSENSITIVITY; ENZYMES; INACTIVATION; ULTRAVIOLET RADIATION; BIOLOGICAL RADIATION EFFECTS; ESCHERICHIA COLI; EXTERNAL IRRADIATION; GALACTOSIDASE; IN VITRO; BACTERIA; BIOLOGICAL EFFECTS; CELL CONSTITUENTS; ELECTROMAGNETIC RADIATION; GLYCOSYL HYDROLASES; HYDROLASES; IRRADIATION; MEMBRANES; MICROORGANISMS; RADIATION EFFECTS; RADIATIONS; 560112* - Radiation Effects on Biochemicals- In Microorganisms- (-1987)
OSTI ID:
5007097
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: PHCBA
Submitting Site:
INIS
Size:
Pages: 379-383
Announcement Date:

Journal Article:

Citation Formats

Robb, F T, and Peak, M J. Inactivation of the lactose permease of Escherichia coli by monochromatic ultraviolet light. United Kingdom: N. p., 1979. Web.
Robb, F T, & Peak, M J. Inactivation of the lactose permease of Escherichia coli by monochromatic ultraviolet light. United Kingdom.
Robb, F T, and Peak, M J. 1979. "Inactivation of the lactose permease of Escherichia coli by monochromatic ultraviolet light." United Kingdom.
@misc{etde_5007097,
title = {Inactivation of the lactose permease of Escherichia coli by monochromatic ultraviolet light}
author = {Robb, F T, and Peak, M J}
abstractNote = {The lactose permease of E. coli was inactivated exponetially by seven wavelengths of monochromatic UV light. An action spectrum revealed that the shorter wavelengths (243, 290 and 313 nm) were much more efficient than longer wavelengths. Inactivation at 290 nm was most efficient and was not due to generalized membrane damage. The rate of counterflux of intracellular ..beta..-galactoside in response to externally added ..beta..-galactoside was slowed by 290 nm irradiation, indicating destruction of the facilitated diffusion mechanism. The induction of ..beta..-galactosidase and ..beta..-galactoside permease was co-ordinate both with and without pre-irradiation by 290 nm light. The ..beta.. galactosidase was approximately 26-fold more resistant to 290 nm than the permease. These results are discussed in terms of a greater sensitivity of membrane proteins to 290 nm light, which may be due to the role of aromatic amino acids in conferring stability to the permease in the membrane.}
journal = {Photochem. Photobiol.; (United Kingdom)}
volume = {3}
journal type = {AC}
place = {United Kingdom}
year = {1979}
month = {Sep}
}