A copper‐transporting P‐type ATPase found in the thylakoid membrane of the cyanobacterium <i>Synechococcus</i> species PCC7942

Molecular Microbiology - Tập 13 Số 2 - Trang 369-377 - 1994
Kengo Kanamaru1,2, Seiji Kashiwagi1, Takeshi Mizuno1
1Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan
2National Institute of Genetics, Yata 1, 111, Mishima, Shizuoka 411 Japan

Tóm tắt

SummaryP‐type ATPases constitute a large family of cation pumps that play crucial physiological roles in many organisms, including bacteria, plants and mammals. They are postulated to play important roles in a variety of environmental adaptation systems. Recently, we cloned two distinct putative P‐type ATPase genes (pacS and pacL) from a photosynthetic cyanobacterium, Synechococcus species PCC7942. in this study, one of the gene products (named PacS) was found to possess a putative metal‐binding motif (Gly‐Met‐X‐Cys‐X‐X‐Cys) in its N‐terminal portion. Thus we supposed that this ATPase may function as a metal pump. Indeed, the results of Northern blotting analysis showed that pacS‐mRNA specifically increases upon addition of copper or silver to the growth medium. The results of Western blotting analysis confirmed the view that PacS accumulates in copper‐treated Synechococcus cells. Thus we concluded that the expression of PacS ATPase is regulated in response to the change in concentration of external metals, namely copper and silver. Consistent with this, an insertional inactivation mutant of pacS exhibited hypersensitivity in terms of growth to these potentially toxic metals, it was also revealed that PacS was mainly located in the thylakoid membrane, in which the photosynthetic reactions take place. This P‐type ATPase in the thylakoid membrane is implicated as a copper‐transporting system that may be involved in copper‐homeostasis crucial to the photosynthetic thylakoid function.

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Tài liệu tham khảo

10.1042/bj1490675

10.1038/263793a0

Asada K., 1987, Photo‐inhibition, 227

10.1104/pp.100.4.1670

Boulter D., 1977, International Review of Biochemistry and Plant Biochemistry Ii, 1

10.1016/0147-619X(92)90005-U

10.1038/ng1293-327

10.1016/0022-2836(87)90667-X

10.1073/pnas.89.18.8716

Hofmann F., 1993, The C‐terminal domain of the plasma membrane Ca2+ pump contains three high affinity Ca2+ binding site, J Biol Chem, 268, 10252, 10.1016/S0021-9258(18)82197-4

10.1111/j.1365-2958.1993.tb01109.x

10.1128/jb.171.2.929-939.1989

10.1016/0014-5793(93)80928-N

10.1007/BF00334390

10.1128/jb.175.14.4492-4498.1993

Matthew J.F., 1994, P‐type ATPase of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees, J Mol Evol, 38, 57, 10.1007/BF00175496

10.1111/j.1365-2958.1992.tb01350.x

10.1111/j.1365-2958.1993.tb01102.x

10.1104/pp.100.3.1471

10.1073/pnas.86.10.3544

10.1128/jb.171.8.4241-4247.1989

Odermatt A., 1993, Primary structure of two P‐type ATPases involved in copper homeostasis in Enteroeoccus hirae, J Biol Chem, 268, 12775, 10.1016/S0021-9258(18)31455-8

Omata T., 1983, Isolation and characterization of the cytoplasmic membranes from the blue–green alga (cyanobacterium), Anacystis nidutans. Plant Cell Physiol, 24, 1101

10.1111/j.1365-2958.1989.tb00172.x

Rippka R., 1979, Genetic assignments, strain histories and properties of pure cultures of cyanobacteria, J Gen Microbiol, 111, 1

10.1111/j.1365-2958.1993.tb00898.x

Skerjanc I.S, 1993, Mutation of glutamate 309 to glutamine alters one Ca2+‐binding site in the Ca2+‐ATPase of sarcoplasmic reticulum expressed in sf9 cells, J Biol Chem, 268, 15944, 10.1016/S0021-9258(18)82343-2

10.1111/j.1365-2958.1992.tb01349.x

10.1038/ng0193-7

10.1073/pnas.89.19.9205

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Molecular Microbiology

Tập 13 Số 2

369-377

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