Show simple item record

dc.contributor.authorMorita, YS
dc.contributor.authorSena, CBC
dc.contributor.authorWaller, RF
dc.contributor.authorKurokawa, K
dc.contributor.authorSernee, MF
dc.contributor.authorNakatani, F
dc.contributor.authorHaites, RE
dc.contributor.authorBillman-Jacobe, H
dc.contributor.authorMcConville, MJ
dc.contributor.authorMaeda, Y
dc.contributor.authorKinoshita, T
dc.date.available2014-05-21T19:21:58Z
dc.date.issued2006-09-01
dc.identifierpii: M604214200
dc.identifier.citationMorita, Y. S., Sena, C. B. C., Waller, R. F., Kurokawa, K., Sernee, M. F., Nakatani, F., Haites, R. E., Billman-Jacobe, H., McConville, M. J., Maeda, Y. & Kinoshita, T. (2006). PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of phosphatidylinositol mannoside in mycobacteria. JOURNAL OF BIOLOGICAL CHEMISTRY, 281 (35), pp.25143-25155. https://doi.org/10.1074/jbc.M604214200.
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/11343/26173
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractPhosphatidylinositol mannosides (PIMs) are a major class of glycolipids in all mycobacteria. AcPIM2, a dimannosyl PIM, is both an end product and a precursor for polar PIMs, such as hexamannosyl PIM (AcPIM6) and the major cell wall lipoglycan, lipoarabinomannan (LAM). The mannosyltransferases that convert AcPIM2 to AcPIM6 or LAM are dependent on polyprenol-phosphate-mannose (PPM), but have not yet been characterized. Here, we identified a gene, termed pimE that is present in all mycobacteria, and is required for AcPIM6 biosynthesis. PimE was initially identified based on homology with eukaryotic PIG-M mannosyltransferases. PimE-deleted Mycobacterium smegmatis was defective in AcPIM6 synthesis, and accumulated the tetramannosyl PIM, AcPIM4. Loss of PimE had no affect on cell growth or viability, or the biosynthesis of other intracellular and cell wall glycans. However, changes in cell wall hydrophobicity and plasma membrane organization were detected, suggesting a role for AcPIM6 in the structural integrity of the cell wall and plasma membrane. These defects were corrected by ectopic expression of the pimE gene. Metabolic pulse-chase radiolabeling and cell-free PIM biosynthesis assays indicated that PimE catalyzes the alpha1,2-mannosyl transfer for the AcPIM5 synthesis. Mutation of an Asp residue in PimE that is conserved in and required for the activity of human PIG-M resulted in loss of PIM-biosynthetic activity, indicating that PimE is the catalytic component. Finally, PimE was localized to a distinct membrane fraction enriched in AcPIM4-6 biosynthesis. Taken together, PimE represents the first PPM-dependent mannosyl-transferase shown to be involved in PIM biosynthesis, where it mediates the fifth mannose transfer.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.subjectCell Metabolism; Biological Sciences
dc.titlePimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of phosphatidylinositol mannoside in mycobacteria
dc.typeJournal Article
dc.identifier.doi10.1074/jbc.M604214200
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentBotany
melbourne.source.titleJOURNAL OF BIOLOGICAL CHEMISTRY
melbourne.source.volume281
melbourne.source.issue35
melbourne.source.pages25143-25155
dc.research.coderfcd270102
dc.research.codeseo1998780105
melbourne.publicationid54393
melbourne.elementsid278795
melbourne.contributor.authorWaller, Ross
melbourne.contributor.authorSernee, Marijke
melbourne.contributor.authorBillman-Jacobe, Helen
melbourne.contributor.authorMcConville, Malcolm
melbourne.contributor.authorHaites, Ruth
dc.identifier.eissn1083-351X
melbourne.accessrightsThis item is currently not available from this repository


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record