Topology and identification of critical residues of the O-acetyltransferase of serotype-converting bacteriophage, SF6, of Shigella flexneri

Farzaana Thanweer, Vikas Tahiliani, Haralambos Korres, Naresh K. Verma*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    15 Citations (SciVal)

    Abstract

    The modification of the LPS O-antigen, seen in the diverse serotypes of Shigella flexneri is brought about by the glucosyltransferases (Gtr) and the O-acetyltransferase (Oac). In this study, we establish the membrane topology of Oac using the dual reporter PhoA-LacZα. We have determined that Oac is an integral membrane protein with 10 transmembrane regions. The hydrophilic N- and C-termini are oriented in the cytoplasm. Functionally important cytoplasmic and periplasmic loops have also been identified. Furthermore, cytoplasmic residues R73 and R75R76 were found to be critical to Oac function.

    Original languageEnglish
    Pages (from-to)581-585
    Number of pages5
    JournalBiochemical and Biophysical Research Communications
    Volume375
    Issue number4
    DOIs
    Publication statusPublished - 31 Oct 2008

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