Ontology highlight
ABSTRACT:
SUBMITTER: Palcekova Z
PROVIDER: S-EPMC6664188 | biostudies-literature | 2019 Jun
REPOSITORIES: biostudies-literature
Palčeková Zuzana Z Angala Shiva K SK Belardinelli Juan Manuel JM Eskandarian Haig A HA Joe Maju M Brunton Richard R Rithner Christopher C Jones Victoria V Nigou Jérôme J Lowary Todd L TL Gilleron Martine M McNeil Michael M Jackson Mary M
The Journal of biological chemistry 20190520 26
Similar to other prokaryotes, mycobacteria decorate their major cell envelope glycans with minor covalent substituents whose biological significance remains largely unknown. We report on the discovery of a mycobacterial enzyme, named here SucT, that adds succinyl groups to the arabinan domains of both arabinogalactan (AG) and lipoarabinomannan (LAM). Disruption of the SucT-encoding gene in <i>Mycobacterium smegmatis</i> abolished AG and LAM succinylation and altered the hydrophobicity and rigidi ...[more]