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dc.contributor.authorKovacevic, S
dc.contributor.authorAnderson, D
dc.contributor.authorMorita, YS
dc.contributor.authorPatterson, J
dc.contributor.authorHaites, R
dc.contributor.authorMcMillan, BNI
dc.contributor.authorCoppel, R
dc.contributor.authorMcConville, MJ
dc.contributor.authorBillman-Jacobe, H
dc.identifierpii: S0021-9258(19)56430-4
dc.identifier.citationKovacevic, S., Anderson, D., Morita, Y. S., Patterson, J., Haites, R., McMillan, B. N. I., Coppel, R., McConville, M. J. & Billman-Jacobe, H. (2006). Identification of a novel protein with a role in lipoarabinomannan biosynthesis in mycobacteria. JOURNAL OF BIOLOGICAL CHEMISTRY, 281 (14), pp.9011-9017.
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractAll species of Mycobacteria synthesize distinctive cell walls that are rich in phosphatidylinositol mannosides (PIMs), lipomannan (LM), and lipoarabinomannan (LAM). PIM glycolipids, having 2-4 mannose residues, can either be channeled into polar PIM species (with 6 Man residues) or hypermannosylated to form LM and LAM. In this study, we have identified a Mycobacterium smegmatis gene, termed lpqW, that is required for the conversion of PIMs to LAM and is highly conserved in all mycobacteria. A transposon mutant, Myco481, containing an insertion near the 3' end of lpqW exhibited altered colony morphology on complex agar medium. This mutant was unstable and was consistently overgrown by a second mutant, represented by Myco481.1, that had normal growth and colony characteristics. Biochemical analysis and metabolic labeling studies showed that Myco481 synthesized the complete spectrum of apolar and polar PIMs but was unable to make LAM. LAM biosynthesis was restored to near wild type levels in Myco481.1. However, this mutant was unable to synthesize the major polar PIM (AcPIM6) and accumulated a smaller intermediate, AcPIM4. Targeted disruption of the lpqW gene and complementation of the initial Myco481 mutant with the wild type gene confirmed that the phenotype of this mutant was due to loss of LpqW. These studies suggest that LpqW has a role in regulating the flux of early PIM intermediates into polar PIM or LAM biosynthesis. They also suggest that AcPIM4 is the likely branch point intermediate in polar PIM and LAM biosynthesis.
dc.subjectBiochemistry and Cell Biology not elsewhere classified ; Biological Sciences
dc.titleIdentification of a novel protein with a role in lipoarabinomannan biosynthesis in mycobacteria
dc.typeJournal Article
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentBiochemistry And Molecular Biology
melbourne.source.titleJournal of Biological Chemistry
melbourne.contributor.authorMcConville, Malcolm
melbourne.contributor.authorBillman-Jacobe, Helen
melbourne.contributor.authorPATTERSON, JOHN
melbourne.contributor.authorANDERSON, DIANNE
melbourne.contributor.authorMORITA, YASUHIRO
melbourne.contributor.authorHAITES, RUTH ELIZABETH
melbourne.contributor.authorMCMILLAN, BENJAMIN NEIL IAN
melbourne.contributor.authorHaites, Ruth
melbourne.accessrightsThis item is currently not available from this repository

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