A Myxococcus xanthus CbpB containing two cAMP-binding domains is involved in temperature and osmotic tolerances.
A Myxococcus xanthus CbpB containing two cAMP-binding domains is involved in temperature and osmotic tolerances.
复制标题
DOI:
10.1016/j.femsle.2005.01.027
复制
发表时间:
2005-03
影响因子:
2.1
通讯作者:
Y. Kimura;H. Nakato;K. Ishibashi;S. Kobayashi
中科院分区:
文献类型:
--
作者:
Y. Kimura;H. Nakato;K. Ishibashi;S. Kobayashi
Our previous data indicated that aMyxococcus xanthussensor-type adenylyl cyclase (CyaA) functions in signal transduction during osmotic stress. However, the cAMP-mediated signal transduction pathway in this bacterium was unknown. Here, we isolated a clone from aM. xanthusgenomic DNA library using oligonucleotide probes designed based on the conserved cAMP-binding domains of the cAMP-dependent protein kinase (PKA) regulatory subunits. The clone contained two open-reading frames (ORFs),cbpAandcbpB, encoding hydrophilic proteins with one and two cAMP-binding domains, respectively. The CbpB exhibited partial primary structural similarity to PKA regulatory subunits.cbpAandcbpBmutants, generated by gene disruption, showed normal growth, development and spore germination. However, thecbpBmutant cultured under high- or low-temperature conditions exhibited a marked reduction in growth.cbpBmutant cells were also more sensitive to osmotic stress than wild-type cells. ThecbpAmutant possessed normal resistance to such stress. The phenotype ofcbpBmutant was similar to those of PKA regulatory subunit mutants of some eukaryotic microorganisms.