Premium
Functional analysis of serine acetyltransferase from Mycobacterium smegmatis
Author(s) -
Qiu Juanjuan,
Ma Yufang,
Owusu Lawrence,
Jiang Tao,
Xin Yi
Publication year - 2014
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201300858
Subject(s) - mycobacterium smegmatis , acetyltransferase , serine , mutant , chemistry , biochemistry , biosynthesis , microbiology and biotechnology , biology , mycobacterium tuberculosis , gene , enzyme , medicine , tuberculosis , pathology , acetylation
Serine acetyltransferase (CysE) is involved in L ‐cysteine biosynthesis in Mycobacterium , and it is important for the self‐defense mechanism of the bacteria. Mycobacterium tuberculosis CysE (Rv2335) has been identified as a serine acetyltransferase, and it is orthologous to Mycobacterium smegmatis MSMEG_5947 . In this study, the MSMEG_5947 gene was cloned, expressed, and identified as a serine acetyltransferase. To investigate the function of M. smegmatis CysE, a MSMEG_5947 knockout mutant strain ( M. sm‐ΔM_5947 ) was generated through homologous recombination. The growth and morphological characteristics of this strain were studied using growth curves and electron microscopy, respectively. M. sm‐ΔM_5947 grew slower than M. smegmatis mc 2 155. Electron microscopy revealed that the lack of the M. smegmatis CysE protein caused drastic morphological changes. Therefore, deletion of the serine acetyltransferase retards the growth of the Mycobacterium , but serine acetyltransferase expression is not essential for the survival of the bacteria.