Cloning and Nucleotide Sequence of Streptococcus pneumoniae ftsH Gene.
- Author:
Hee Soo KIM
;
Jae Man CHUNG
;
Eun Hee LEE
;
Yeong Hwan HAN
- Publication Type:Original Article
- MeSH:
Amino Acid Sequence;
ATP-Dependent Proteases;
Base Sequence*;
Clone Cells*;
Cloning, Organism*;
Cytoplasm;
DNA;
Escherichia coli;
Gram-Positive Bacteria;
Lactococcus lactis;
Polymerase Chain Reaction;
Promoter Regions, Genetic;
Streptococcus pneumoniae*;
Streptococcus*;
Strikes, Employee
- From:Journal of the Korean Society for Microbiology
1999;34(2):115-123
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
The gene ftsH encodes a membrane-bound and ATP-dependent protease that is involved in a variety of cellular functions including heat-shock and stress response. Streptococcus pneumoniae DNA encompassing most part of the ftsH gene was cloned in Escherichia coli and sequenced. Due to the unsuccessful cloning as seen in other pneumococcal promoters, the 5'-end of the gene including the upstream promoter region was amplified by inverse polymerase chain reaction and then sequenced by cyclic sequencing. The amino acid sequence that is deduced from the 1,959 bp-long ftsH gene is very similar to FtsH of several gram-positive bacteria and E. coli within the region responsible for the AAA (ATPase associated with diverse cellular activities) function. Except for the N-terminal domain that contains a short extracellular region between two mernbrane-spanning segments, pneumococcal FtsH shows striking sequence similarity to that of a closely related species Lactococcus lactis within the conserved cytoplasmic domain where two ATP-binding motifs, the AAA Signature motif, and a zinc-binding motif are found.
