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Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile

View Article: PubMed Central - PubMed

ABSTRACT

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.

No MeSH data available.


MSA of repeat Set #3. Residues are colored according to the predicted secondary structures: red, α-helix; blue, β-strand; yellow, coil; and white, ambiguous. The consensus secondary structure is βββα shown at the bottom. The subsequences are listed in order of their E-values. The YGF motif is denoted by a black bar on the top line. GLI and MYPU denote Gli349 and MYPU2110, respectively, and the following number denotes the repeat start position in each subsequence. Residue numbering is the same as in Fig. 4.
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f5-1_33: MSA of repeat Set #3. Residues are colored according to the predicted secondary structures: red, α-helix; blue, β-strand; yellow, coil; and white, ambiguous. The consensus secondary structure is βββα shown at the bottom. The subsequences are listed in order of their E-values. The YGF motif is denoted by a black bar on the top line. GLI and MYPU denote Gli349 and MYPU2110, respectively, and the following number denotes the repeat start position in each subsequence. Residue numbering is the same as in Fig. 4.

Mentions: The predicted secondary structure of each repeat, determined using the NPS server (http://npsa-pbil.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_seccons.html)26, was found to be βββα with the second β-strand being well conserved among all repeats (Fig. 5). The locations of the predicted β-strands are particularly consistent with the binary pattern, which suggests the existence of three β-strands. The most highly conserved residues in the YGF motif, Gly and Phe, are found in the region extending from the middle of the third β-strand to the beginning of the following α-helix. Both the primary and secondary structures of the region are well conserved, which may suggest that those regions are important for determining the structure of Gli349. The secondary structure near the C-terminus is less conserved (Fig. 5), suggesting this region may be a linker between domains. The characteristics of the predicted secondary structures of the repeats in MYPU2110 are similar to those of Gli349.


Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile
MSA of repeat Set #3. Residues are colored according to the predicted secondary structures: red, α-helix; blue, β-strand; yellow, coil; and white, ambiguous. The consensus secondary structure is βββα shown at the bottom. The subsequences are listed in order of their E-values. The YGF motif is denoted by a black bar on the top line. GLI and MYPU denote Gli349 and MYPU2110, respectively, and the following number denotes the repeat start position in each subsequence. Residue numbering is the same as in Fig. 4.
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Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC5036628&req=5

f5-1_33: MSA of repeat Set #3. Residues are colored according to the predicted secondary structures: red, α-helix; blue, β-strand; yellow, coil; and white, ambiguous. The consensus secondary structure is βββα shown at the bottom. The subsequences are listed in order of their E-values. The YGF motif is denoted by a black bar on the top line. GLI and MYPU denote Gli349 and MYPU2110, respectively, and the following number denotes the repeat start position in each subsequence. Residue numbering is the same as in Fig. 4.
Mentions: The predicted secondary structure of each repeat, determined using the NPS server (http://npsa-pbil.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_seccons.html)26, was found to be βββα with the second β-strand being well conserved among all repeats (Fig. 5). The locations of the predicted β-strands are particularly consistent with the binary pattern, which suggests the existence of three β-strands. The most highly conserved residues in the YGF motif, Gly and Phe, are found in the region extending from the middle of the third β-strand to the beginning of the following α-helix. Both the primary and secondary structures of the region are well conserved, which may suggest that those regions are important for determining the structure of Gli349. The secondary structure near the C-terminus is less conserved (Fig. 5), suggesting this region may be a linker between domains. The characteristics of the predicted secondary structures of the repeats in MYPU2110 are similar to those of Gli349.

View Article: PubMed Central - PubMed

ABSTRACT

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.

No MeSH data available.