A murein-bound form of prolipoprotein was found in the cell envelope fraction of globomycin-treated Escherichia coli B. We suggest therefore that proteolytic cleavage of prolipoprotein to mature lipoprotein is not essential for the transpeptidation of the lipoprotein to peptidoglycan.
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http://dx.doi.org/10.1128/jb.140.3.1098-1101.1979 | DOI Listing |
Biochem Biophys Res Commun
June 2017
Centre for Biotechnology, Anna University, Chennai, India.
Bacterial lipid modification of proteins is an essential post-translational event committed by Phosphatidylglycerol: prolipoprotein diacylglyceryl transferase (Lgt) by catalysing diacyglyceryl transfer from Phosphatidylglycerol to cysteine present in the characteristic 'lipobox' ([LVI] [ASTVI] [GAS] C ) of prolipoprotein signal peptides. This is then followed by the cleavage of the signal peptide by lipoprotein-specific signal peptidase (LspA). It had been known for long that threonine at the -1 position allows diacylglyceryl modification by Lgt, but not signal peptide cleavage by LspA.
View Article and Find Full Text PDFNat Commun
January 2016
National Laboratory of Macromolecules, National Center of Protein Science - Beijing, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
Lipoprotein biogenesis is essential for bacterial survival. Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) is an integral membrane enzyme that catalyses the first reaction of the three-step post-translational lipid modification. Deletion of the lgt gene is lethal to most Gram-negative bacteria.
View Article and Find Full Text PDFGene
April 2015
Department of Microbiology, Vallabhbhai Patel Chest Institute, University of Delhi, Delhi 110007, India. Electronic address:
Lipoprotein signal peptidase, lspA (Rv1539), is the only known gene in mycobacterial genome for cleaving the signal sequence from prolipoprotein to form mature lipoprotein. It has been implicated in maintaining the virulence of Mycobacterium tuberculosis. The regulation of lspA had not been studied so far.
View Article and Find Full Text PDFProtein Expr Purif
February 2013
Centre for Biotechnology, Anna University, Chennai 600 025, India.
The unique bacterial enzyme phosphatidylglycerol: prolipoprotein diacylglyceryl transferase (Lgt) is the least studied enzyme of the ubiquitous bacterial lipoprotein synthetic pathway, mostly due to the low abundance of the enzyme. So far, Lgt has been studied to a limited extent in gram-negative bacteria, mainly in Escherichia coli. We, for the first time, report the isolation of an adequate amount of Lgt from the gram-positive lactic acid bacteria, Lactococcus lactis and compare this wild-type bacterial enzyme with the E.
View Article and Find Full Text PDFMicrobiology (Reading)
May 2012
Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-ohkubo, Sakura-ku, Saitama-shi, Saitama-ken 338-8570, Japan.
The Rcs phosphorelay signal transduction system controls genes for capsule production and many other envelope-related functions and is implicated in biofilm formation. We investigated the activation of the Rcs system in a pgsA null mutant of Escherichia coli, which completely lacks the major acidic phospholipids phosphatidylglycerol and cardiolipin. We found that the Rcs activation, and consequent thermosensitivity, were suppressed by overexpression of the lgt gene, encoding diacylglyceryltransferase, which catalyses the modification of prolipoproteins that is the first step in the maturation and localization process of lipoproteins, and is a prerequisite for the later steps.
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