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Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile
The motile mechanism of Mycoplasma mobile remains unknown but is believed to differ from any previously identified mechanism in bacteria. Gli349 of M. mobile is known to be responsible for both adhesion to glass surfaces and mobility. We therefore carried out sequence analyses of Gli349 and its homo...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society of Japan (BSJ)
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036628/ https://www.ncbi.nlm.nih.gov/pubmed/27857551 http://dx.doi.org/10.2142/biophysics.1.33 |
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author | Metsugi, Shoichi Uenoyama, Atsuko Adan-Kubo, Jun Miyata, Makoto Yura, Kei Kono, Hidetoshi Go, Nobuhiro |
author_facet | Metsugi, Shoichi Uenoyama, Atsuko Adan-Kubo, Jun Miyata, Makoto Yura, Kei Kono, Hidetoshi Go, Nobuhiro |
author_sort | Metsugi, Shoichi |
collection | PubMed |
description | The motile mechanism of Mycoplasma mobile remains unknown but is believed to differ from any previously identified mechanism in bacteria. Gli349 of M. mobile is known to be responsible for both adhesion to glass surfaces and mobility. We therefore carried out sequence analyses of Gli349 and its homolog MYPU2110 from M. pulmonis to decipher their structures. We found that the motif “YxxxxxGF” appears 11 times in Gli349 and 16 times in MYPU2110. Further analysis of the sequences revealed that Gli349 contains 18 repeats of about 100 amino acid residues each, and MYPU2110 contains 22. No sequence homologous to any of the repeats was found in the NCBI RefSeq non-redundant sequence database, and no compatible fold structure was found among known protein structures, suggesting that the repeat found in Gli349 and MYPU2110 is novel and takes a new fold structure. Proteolysis of Gli349 using chymotrypsin revealed that cleavage positions were often located between the repeats, implying that regions connecting repeats are unstructured, flexible and exposed to the solvent. Assuming that each repeat folds into a structural domain, we constructed a model of Gli349 that fits well the shape and size of images obtained with electron microscopy. |
format | Online Article Text |
id | pubmed-5036628 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
spelling | pubmed-50366282016-11-17 Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile Metsugi, Shoichi Uenoyama, Atsuko Adan-Kubo, Jun Miyata, Makoto Yura, Kei Kono, Hidetoshi Go, Nobuhiro Biophysics (Nagoya-shi) Articles The motile mechanism of Mycoplasma mobile remains unknown but is believed to differ from any previously identified mechanism in bacteria. Gli349 of M. mobile is known to be responsible for both adhesion to glass surfaces and mobility. We therefore carried out sequence analyses of Gli349 and its homolog MYPU2110 from M. pulmonis to decipher their structures. We found that the motif “YxxxxxGF” appears 11 times in Gli349 and 16 times in MYPU2110. Further analysis of the sequences revealed that Gli349 contains 18 repeats of about 100 amino acid residues each, and MYPU2110 contains 22. No sequence homologous to any of the repeats was found in the NCBI RefSeq non-redundant sequence database, and no compatible fold structure was found among known protein structures, suggesting that the repeat found in Gli349 and MYPU2110 is novel and takes a new fold structure. Proteolysis of Gli349 using chymotrypsin revealed that cleavage positions were often located between the repeats, implying that regions connecting repeats are unstructured, flexible and exposed to the solvent. Assuming that each repeat folds into a structural domain, we constructed a model of Gli349 that fits well the shape and size of images obtained with electron microscopy. The Biophysical Society of Japan (BSJ) 2005-05-25 /pmc/articles/PMC5036628/ /pubmed/27857551 http://dx.doi.org/10.2142/biophysics.1.33 Text en 2005 © The Biophysical Society of Japan |
spellingShingle | Articles Metsugi, Shoichi Uenoyama, Atsuko Adan-Kubo, Jun Miyata, Makoto Yura, Kei Kono, Hidetoshi Go, Nobuhiro Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile |
title | Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile |
title_full | Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile |
title_fullStr | Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile |
title_full_unstemmed | Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile |
title_short | Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile |
title_sort | sequence analysis of the gliding protein gli349 in mycoplasma mobile |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036628/ https://www.ncbi.nlm.nih.gov/pubmed/27857551 http://dx.doi.org/10.2142/biophysics.1.33 |
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