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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.


Multiple sequence alignment of 10 subsequences of Gli349 containing a YGF motif is shown. The start and end positions of each repeat are denoted in the first column. Colors on the sequences denote as follows: yellow, 100% conserved residues; cyan, >50% conserved residues; orange, sites that are >70% conserved for D, N, S and T; green, sites that are >70% conserved for A, I, L and V.
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f1-1_33: Multiple sequence alignment of 10 subsequences of Gli349 containing a YGF motif is shown. The start and end positions of each repeat are denoted in the first column. Colors on the sequences denote as follows: yellow, 100% conserved residues; cyan, >50% conserved residues; orange, sites that are >70% conserved for D, N, S and T; green, sites that are >70% conserved for A, I, L and V.

Mentions: Notably, the positions of the Y within the YGF motif in Gli349 are 867, 979, 1087, 1588, 1694, 1801, 2009, 2123, 2322 and 2653; those in MYPU2110 are 138, 962, 1066, 1363, 1464, 1679, 1775, 1872, 1977, 2081, 2289, 2415 and 2640. Thus each YGF motif is separated by a multiple of about 100 (100, 200, 300 ...) amino acid residues, which implies the existence of a repeat whose length is a multiple of 100. When we took the greatest common measure (i.e., 100) as the repeat length, we found there to be 10 subsequences of about 100 residues in Gli349 and 13 subsequences in MYPU2110 that were well aligned and had several conserved sites in addition to the YGF motif. E-values of each pair-wise alignment of the sequences in Table 1 range from 1×10−6 to 3.4. Figure 1 shows the MSA of the 10 subsequences in Gli349 generated using clustalW21,22. Note that the region around the YGF motif is conserved best.


Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile
Multiple sequence alignment of 10 subsequences of Gli349 containing a YGF motif is shown. The start and end positions of each repeat are denoted in the first column. Colors on the sequences denote as follows: yellow, 100% conserved residues; cyan, >50% conserved residues; orange, sites that are >70% conserved for D, N, S and T; green, sites that are >70% conserved for A, I, L and V.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC5036628&req=5

f1-1_33: Multiple sequence alignment of 10 subsequences of Gli349 containing a YGF motif is shown. The start and end positions of each repeat are denoted in the first column. Colors on the sequences denote as follows: yellow, 100% conserved residues; cyan, >50% conserved residues; orange, sites that are >70% conserved for D, N, S and T; green, sites that are >70% conserved for A, I, L and V.
Mentions: Notably, the positions of the Y within the YGF motif in Gli349 are 867, 979, 1087, 1588, 1694, 1801, 2009, 2123, 2322 and 2653; those in MYPU2110 are 138, 962, 1066, 1363, 1464, 1679, 1775, 1872, 1977, 2081, 2289, 2415 and 2640. Thus each YGF motif is separated by a multiple of about 100 (100, 200, 300 ...) amino acid residues, which implies the existence of a repeat whose length is a multiple of 100. When we took the greatest common measure (i.e., 100) as the repeat length, we found there to be 10 subsequences of about 100 residues in Gli349 and 13 subsequences in MYPU2110 that were well aligned and had several conserved sites in addition to the YGF motif. E-values of each pair-wise alignment of the sequences in Table 1 range from 1×10−6 to 3.4. Figure 1 shows the MSA of the 10 subsequences in Gli349 generated using clustalW21,22. Note that the region around the YGF motif is conserved best.

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.