Characterization of the Mycoplasma hominis ftsZ gene and its sequence variability in mycoplasma clinical isolates

We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse transcription followed by PCR amplification. We revealed that M. hominis FtsZ had a comparatively low similarity to proteins of Mycoplasma geni...

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Published inBiochemical and biophysical research communications Vol. 293; no. 1; pp. 155 - 162
Main Authors Momynaliev, K.T, Smirnova, O.V, Lazyrev, V.N, Akopian, T.A, Chelysheva, V.V, Ayala, J.A, Simankova, A.N, Borchsenius, S.N, Govorun, V.M
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Published United States Elsevier Inc 26.04.2002
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Abstract We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse transcription followed by PCR amplification. We revealed that M. hominis FtsZ had a comparatively low similarity to proteins of Mycoplasma genitalium and Mycoplasma pneumoniae. After full ftsZ gene sequencing for 14 clinical isolates of M. hominis, single-nucleotide substitutions were found in 21 positions, 6 of them being common for almost all isolates. This ftsZ gene polymorphism may be used for subtyping of M. hominis in clinical samples. Expression of the M. hominis ftsZ gene in different Escherichia coli strains was also demonstrated, and M. hominis FtsZ protein was purified from E. coli cells transformed with recombinant expression plasmid. Complementation between the M. hominis FtsZ and E. coli FtsZ could be shown. The comparison of FtsZ protein structures may also be used for investigation of bacterial phylogenetic relationships.
AbstractList We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse transcription followed by PCR amplification. We revealed that M. hominis FtsZ had a comparatively low similarity to proteins of Mycoplasma genitalium and Mycoplasma pneumoniae. After full ftsZ gene sequencing for 14 clinical isolates of M. hominis, single-nucleotide substitutions were found in 21 positions, 6 of them being common for almost all isolates. This ftsZ gene polymorphism may be used for subtyping of M. hominis in clinical samples. Expression of the M. hominis ftsZ gene in different Escherichia coli strains was also demonstrated, and M. hominis FtsZ protein was purified from E. coli cells transformed with recombinant expression plasmid. Complementation between the M. hominis FtsZ and E. coli FtsZ could be shown. The comparison of FtsZ protein structures may also be used for investigation of bacterial phylogenetic relationships.
We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse transcription followed by PCR amplification. We revealed that M. hominis FtsZ had a comparatively low similarity to proteins of Mycoplasma genitalium and Mycoplasma pneumoniae. After full ftsZ gene sequencing for 14 clinical isolates of M. hominis, single-nucleotide substitutions were found in 21 positions, 6 of them being common for almost all isolates. This ftsZ gene polymorphism may be used for subtyping of M. hominis in clinical samples. Expression of the M. hominis ftsZ gene in different Escherichia coli strains was also demonstrated, and M. hominis FtsZ protein was purified from E. coli cells transformed with recombinant expression plasmid. Complementation between the M. hominis FtsZ and E. coli FtsZ could be shown. The comparison of FtsZ protein structures may also be used for investigation of bacterial phylogenetic relationships.
We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse transcription followed by PCR amplification. We revealed that M. hominis FtsZ had a comparatively low similarity to proteins of Mycoplasma genitalium and Mycoplasma pneumoniae. After full ftsZ gene sequencing for 14 clinical isolates of M. hominis, single-nucleotide substitutions were found in 21 positions, 6 of them being common for almost all isolates. ThisftsZ gene polymorphism may be used for subtyping of M. hominis in clinical samples. Expression of the M. hominis ftsZ gene in different Escherichia coli strains was also demonstrated, andM. hominis FtsZ protein was purified from E. coli cells transformed with recombinant expression plasmid. Complementation between theM. hominis FtsZ and E. coli FtsZ could be shown. The comparison of FtsZ protein structures may also be used for investigation of bacterial phylogenetic relationships. [copy ] 2002 Elsevier Science (USA)
Author Lazyrev, V.N
Govorun, V.M
Momynaliev, K.T
Simankova, A.N
Chelysheva, V.V
Ayala, J.A
Akopian, T.A
Borchsenius, S.N
Smirnova, O.V
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Keywords ftsZ Gene
Bacterial evolution
Mycoplasma
Gene expression
M. hominis
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Snippet We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse...
We cloned and sequenced Mycoplasma hominis chromosomal fragment containing ftsZ gene. The wild-type expression of the gene was shown at RNA level by reverse...
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SubjectTerms Amino Acid Sequence
Bacterial evolution
Bacterial Proteins - genetics
Base Sequence
Chromosome Mapping
Chromosomes, Bacterial - genetics
Cloning, Molecular
Cytoskeletal Proteins
Escherichia coli - genetics
ftsZ Gene
Gene expression
Genes, Bacterial
Genetic Variation
GTP Phosphohydrolases - genetics
M. hominis
Molecular Sequence Data
Mycoplasma
Mycoplasma hominis - genetics
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Title Characterization of the Mycoplasma hominis ftsZ gene and its sequence variability in mycoplasma clinical isolates
URI https://dx.doi.org/10.1016/S0006-291X(02)00184-5
https://www.ncbi.nlm.nih.gov/pubmed/12054578
https://search.proquest.com/docview/18402765
https://search.proquest.com/docview/71798222
Volume 293
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