Premium
Primary and alternative S18 ribosomal protein in Mycobacterium tuberculosis
Author(s) -
Prisic Sladjana,
Husson Robert N.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.986.8
Subject(s) - ribosomal protein , ribosome , mycobacterium tuberculosis , ribosome biogenesis , ribosomal rna , operon , chemistry , biology , microbiology and biotechnology , biochemistry , rna , tuberculosis , gene , mutant , medicine , pathology
Protein synthesis is a tightly regulated process in every living organism and is likely to be a point of control in Mycobacterium tuberculosis ( Mtb ) during the course of infection. Mtb has four alternative ribosomal proteins organized in a single operon, whose function is not known, but may play an important role in translation regulation. Intriguingly, one of these proteins, S18–2, and its primary ribosomal protein paralog, S18–1, are both phosphorylated in vivo. Measured by their ability to bind another protein in a course of a ribosome biogenesis, their activities are not affected by phosphorylation, but it changes their stability in vitro. This possibly helps the exchange in response to zinc concentration, which regulates (represses) only expression of S18–2. In addition, presence of zinc had a profound and opposed effect on in vitro activities of S18–1 and S18–2 proteins, i.e., zinc activates S18–1 and inhibits S18–2. These data together suggest a model in which S18–1 is able to be a dominant ribosome constituent in high zinc conditions, but that it may be replaced by S18–2 when zinc is deficient. Therefore, S18–2 and other alternative ribosomal proteins may play a role in Mtb viability in necrotizing granulomas, which are thought to be a low zinc environment and are important for TB transmission.