Molecular characterization of the Borrelia burgdorferi in vivo-essential protein PncA

    Authors

    M. W. Jewett; S. Jain; A. K. Linowski; A. Sarkar;P. A. Rosa

    Comments

    Authors: contact us about adding a copy of your work at STARS@ucf.edu

    Abbreviated Journal Title

    Microbiology-(UK)

    Keywords

    LYME-DISEASE SPIROCHETE; LIFE-SPAN EXTENSION; ESCHERICHIA-COLI; SACCHAROMYCES-CEREVISIAE; NICOTINAMIDASE PNCA; CALORIE RESTRICTION; INITIATION CODON; INFECTIOUS CYCLE; GENE; IDENTIFICATION; Microbiology

    Abstract

    The conversion of nicotinamide to nicotinic acid by nicotinamidase enzymes is a critical step in maintaining NAD(+) homeostasis and contributes to numerous important biological processes in diverse organisms. In Borrelia burgdorferi, the nicotinamidase enzyme, PncA, is required for spirochaete survival throughout the infectious cycle. Mammals lack nicotinamidases and therefore PncA may serve as a therapeutic target for Lyme disease. Contrary to the in vivo importance of PncA, the current annotation for the pncA ORF suggests that the encoded protein may be inactive due to the absence of an N-terminal aspartic acid residue that is a conserved member of the catalytic triad of characterized PncA proteins. Herein, we have used genetic and biochemical strategies to determine the N-terminal sequence of B. burgdorferi PncA. Our data demonstrate that the PncA protein is 24 aa longer than the currently annotated sequence and that pncA translation is initiated from the rare, non-canonical initiation codon AUU. These findings are an important first step in understanding the catalytic function of this in vivo-essential protein.

    Journal Title

    Microbiology-Sgm

    Volume

    157

    Publication Date

    1-1-2011

    Document Type

    Article

    Language

    English

    First Page

    2831

    Last Page

    2840

    WOS Identifier

    WOS:000296177300009

    ISSN

    1350-0872

    Share

    COinS