The Cyanobacterial PilT Protein Responsible for Cell Motility and Transformation Hydrolyzes ATP
The unicellular cyanobacterium, Synechocystis sp. PCC 6803 is motile. A homologue of the PilT protein family, required for twitching motility in Pseudomonas aeruginosa and social gliding motility in Myxococcus xanthus, was found to be necessarily associated with cyanobacterial motility. The pilT1 (s...
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Published in | Plant and cell physiology Vol. 43; no. 10; pp. 1127 - 1136 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Japan
Oxford University Press
01.10.2002
Oxford Publishing Limited (England) |
Subjects | |
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Abstract | The unicellular cyanobacterium, Synechocystis sp. PCC 6803 is motile. A homologue of the PilT protein family, required for twitching motility in Pseudomonas aeruginosa and social gliding motility in Myxococcus xanthus, was found to be necessarily associated with cyanobacterial motility. The pilT1 (slr0161) mutant shows a pleotropic phenotype, defects in individual cell motility, and an increased number of long surface pili. Furthermore, the mutant loses its ability of natural competency. These findings demonstrate that PilT1 is essential for both cell motility and competency. Since the pilT gene contains a consensus ATP-binding motif (Walker boxes), the PilT protein is suggested for supplying energy for cell motility. The product of pilT1, overproduced in Escherichia coli and purified by Ni-affinity chromatography, hydrolyzes ATP in vitro. |
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AbstractList | The unicellular cyanobacterium, Synechocystis sp. PCC 6803 is motile. A homologue of the PilT protein family, required for twitching motility in Pseudomonas aeruginosa and social gliding motility in Myxococcus xanthus, was found to be necessarily associated with cyanobacterial motility. The pilT1 (slr0161) mutant shows a pleotropic phenotype, defects in individual cell motility, and an increased number of long surface pili. Furthermore, the mutant loses its ability of natural competency. These findings demonstrate that PilT1 is essential for both cell motility and competency. Since the pilT gene contains a consensus ATP-binding motif (Walker boxes), the PilT protein is suggested for supplying energy for cell motility. The product of pilT1, overproduced in Escherichia coli and purified by Ni-affinity chromatography, hydrolyzes ATP in vitro. |
Author | Ohmori, Masayuki Okamoto, Shinobu |
Author_xml | – sequence: 1 givenname: Shinobu surname: Okamoto fullname: Okamoto, Shinobu – sequence: 2 givenname: Masayuki surname: Ohmori fullname: Ohmori, Masayuki |
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Snippet | The unicellular cyanobacterium, Synechocystis sp. PCC 6803 is motile. A homologue of the PilT protein family, required for twitching motility in Pseudomonas... |
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SubjectTerms | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - isolation & purification Adenosine Triphosphatases - metabolism Adenosine Triphosphate Amino Acid Sequence Bacterial Proteins Chromatography, Affinity Conserved Sequence - genetics Cyanobacteria - genetics Cyanobacteria - metabolism Cyanobacteria - ultrastructure Escherichia coli - genetics Escherichia coli - metabolism Fimbriae, Bacterial - genetics Fimbriae, Bacterial - metabolism Gene Expression Regulation, Bacterial IPTG isopropyl-β-d-(–)-thiogalactopyranoside Keywords: ATPase — Cyanobacteria — Motility — Pili — pilT Microscopy, Electron Molecular Motor Proteins - genetics Molecular Motor Proteins - isolation & purification Molecular Motor Proteins - metabolism Molecular Sequence Data Mutation phenylmethanesulfonyl fluoride PMSF |
Title | The Cyanobacterial PilT Protein Responsible for Cell Motility and Transformation Hydrolyzes ATP |
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