Project/Area Number |
63044113
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Research Category |
Grant-in-Aid for international Scientific Research
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Allocation Type | Single-year Grants |
Section | Joint Research |
Research Institution | Kumamoto University |
Principal Investigator |
HIRAGA Sota Kumamoto Univ. Medical School Professor, 医学部, 教授 (40027321)
|
Co-Investigator(Kenkyū-buntansha) |
ブロック フィリップ ハ゜リ大学, ジャクモノ研究所, 助手
ロビン アリーヌ ハ゜リ大学, ジャクモノ研究所, 講師
ジョスリン ダニエル ハ゜リ大学, ジャクモノ研究所, 講師
リーバード ジャンクロー ハ゜リ大学, ジャクモノ研究所, 講師
ジャフェ アリーヌ ハ゜リ大学, ジャクモノ研究所, 助教授
ダリ リチャード ハ゜リ大学, ジャクモノ研究所, 教授
NIKI Hironori Kumamoto Univ. Medical School, Instructor, 医学部, 助手 (70208122)
OGURA Teru Kumamoto Univ. Medical School, Associate Professor, 医学部, 助教授 (00158825)
BOULOC Philippe Jaques Monod Institute, Instructor
ROBIN Aline Jaques Monod Institute, Lecturer
JOSELEAN Daniele Jaques Menod Institute, Lecturer
LIEBARD Jean-Claude Jaques Monod Institute, Lecturer
DARI Richard Jaques Monod Institute, Professor
JAFFE Aline Jaques Monod Institute, Professor
|
Project Period (FY) |
1988 – 1990
|
Project Status |
Completed (Fiscal Year 1990)
|
Budget Amount *help |
¥9,000,000 (Direct Cost: ¥9,000,000)
Fiscal Year 1990: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1989: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1988: ¥3,000,000 (Direct Cost: ¥3,000,000)
|
Keywords | Chromosome partitioning / Chromosome positioning / mukA gene / mukB gene / Cell division / Morphogenesis / ftsH gene / Protein translocation |
Research Abstract |
We have on studied mechanisms for chromosome partitioning and cell division in E. coli. The positioning of replicated chromosomes at the cell quarters was inhibited when protein synthesis was inhibited. We have isolated a novel type of mutants which forms anucleate cells. One of them, named mukAI, is not lethal and produces normal-sized anucleate cells, The mutant is defective in the chromosome positioning, resulting in production of one anucleate daughter cell and one with two chromosomes. It was indicated that the mukA gene is identical to the tolC gene encoding an outer membrane protein. A nother mutant shows aberrant chromosome partitioning at low temperature, and cannot form colonies and nucleoids are distributed irregularly at high temperature. The mutant is defective in a gene, named mukB, located at 21 min. The mukB gene codes for a protein of 177 kDa. The predicted MukB protein has distinct domains : an amino-terminal globular domain containing a nucleotide-binding sequence, a central region containing two alpha-helical coiled-coil domains and one globular domain, and a corboxyl-terminal globular domain which is rich in Cys, Arg and Lys. The amino-terminal domain of the MukB protein is homologous with that of the microtubule-associated enzyme dynamin (D100) of rat brain. Penicillin-binding protein 2 (PBP2) is required for rod morphology. A new thermosensitive PBP2 allele and an vitro-constructed deletion allele were shown to be lethal in wild-type strains, suggesting that the activity of PBP2 is essential for growth and division. The ftsH mutant shows thermosensitive filamentation with reduced amounts of PBP3. Maturation of prePBP3 is inhibited in the mutant. FtsH protein was deduced to be a membrane protein of 71 kDa which has an ATP-binding domain. Highly significant homology was observed between FtsH protein and a novel family of eukaryotic ATPases including yeast Sec18p, which is involved in protein transport pathways.
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