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Core proteome of the minimal cell: comparative proteomics of three mollicute species.

Fisunov GY, Alexeev DG, Bazaleev NA, Ladygina VG, Galyamina MA, Kondratov IG, Zhukova NA, Serebryakova MV, Demina IA, Govorun VM - PLoS ONE (2011)

Bottom Line: We also obtained a genome core of the respective organisms and compared it with the proteome core.It was found that the genome core encodes 73 more proteins than the proteome core.Apart of proteins which may not be identified due to technical limitations, there are 24 proteins that seem to not be expressed under the optimal conditions.

View Article: PubMed Central - PubMed

Affiliation: Scientific Research Institute of Physical-Chemical Medicine, Federal Bio-Medical Agency of Russia, Moscow, Russia. herr.romanoff@gmail.com

ABSTRACT
Mollicutes (mycoplasmas) have been recognized as highly evolved prokaryotes with an extremely small genome size and very limited coding capacity. Thus, they may serve as a model of a 'minimal cell': a cell with the lowest possible number of genes yet capable of autonomous self-replication. We present the results of a comparative analysis of proteomes of three mycoplasma species: A. laidlawii, M. gallisepticum, and M. mobile. The core proteome components found in the three mycoplasma species are involved in fundamental cellular processes which are necessary for the free living of cells. They include replication, transcription, translation, and minimal metabolism. The members of the proteome core seem to be tightly interconnected with a number of interactions forming core interactome whether or not additional species-specific proteins are located on the periphery. We also obtained a genome core of the respective organisms and compared it with the proteome core. It was found that the genome core encodes 73 more proteins than the proteome core. Apart of proteins which may not be identified due to technical limitations, there are 24 proteins that seem to not be expressed under the optimal conditions.

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Core proteins interaction chart based on M. pneumoniae and B. subtilis data.Proteins are divided to groups: DNA handling, transcription, translation, chaperones, glycolysis. Yellow indicates membrane-bound proteins of M pneumonia that interact with core proteins. ENO, PGK, S2 and L5 are found in a large number of bacterial species.
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pone-0021964-g005: Core proteins interaction chart based on M. pneumoniae and B. subtilis data.Proteins are divided to groups: DNA handling, transcription, translation, chaperones, glycolysis. Yellow indicates membrane-bound proteins of M pneumonia that interact with core proteins. ENO, PGK, S2 and L5 are found in a large number of bacterial species.

Mentions: Based on M. pneumonia and B. subtilis protein complexes data, it is possible to estimate the composition of protein complexes in the proteome core. The interactions among selected members of the proteome core are displayed in Figure 5. Proteins of the proteome core form multifunctional complexes. For example, phosphoglycerate kinase, enolase, and two ribosomal proteins (S2 and L5), according to Commichau et al [25], form interactional bridges between glycolysis, a translation apparatus; chaperones hold together glycolysis, translation, transcription, and DNA-binding proteins.


Core proteome of the minimal cell: comparative proteomics of three mollicute species.

Fisunov GY, Alexeev DG, Bazaleev NA, Ladygina VG, Galyamina MA, Kondratov IG, Zhukova NA, Serebryakova MV, Demina IA, Govorun VM - PLoS ONE (2011)

Core proteins interaction chart based on M. pneumoniae and B. subtilis data.Proteins are divided to groups: DNA handling, transcription, translation, chaperones, glycolysis. Yellow indicates membrane-bound proteins of M pneumonia that interact with core proteins. ENO, PGK, S2 and L5 are found in a large number of bacterial species.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3139596&req=5

pone-0021964-g005: Core proteins interaction chart based on M. pneumoniae and B. subtilis data.Proteins are divided to groups: DNA handling, transcription, translation, chaperones, glycolysis. Yellow indicates membrane-bound proteins of M pneumonia that interact with core proteins. ENO, PGK, S2 and L5 are found in a large number of bacterial species.
Mentions: Based on M. pneumonia and B. subtilis protein complexes data, it is possible to estimate the composition of protein complexes in the proteome core. The interactions among selected members of the proteome core are displayed in Figure 5. Proteins of the proteome core form multifunctional complexes. For example, phosphoglycerate kinase, enolase, and two ribosomal proteins (S2 and L5), according to Commichau et al [25], form interactional bridges between glycolysis, a translation apparatus; chaperones hold together glycolysis, translation, transcription, and DNA-binding proteins.

Bottom Line: We also obtained a genome core of the respective organisms and compared it with the proteome core.It was found that the genome core encodes 73 more proteins than the proteome core.Apart of proteins which may not be identified due to technical limitations, there are 24 proteins that seem to not be expressed under the optimal conditions.

View Article: PubMed Central - PubMed

Affiliation: Scientific Research Institute of Physical-Chemical Medicine, Federal Bio-Medical Agency of Russia, Moscow, Russia. herr.romanoff@gmail.com

ABSTRACT
Mollicutes (mycoplasmas) have been recognized as highly evolved prokaryotes with an extremely small genome size and very limited coding capacity. Thus, they may serve as a model of a 'minimal cell': a cell with the lowest possible number of genes yet capable of autonomous self-replication. We present the results of a comparative analysis of proteomes of three mycoplasma species: A. laidlawii, M. gallisepticum, and M. mobile. The core proteome components found in the three mycoplasma species are involved in fundamental cellular processes which are necessary for the free living of cells. They include replication, transcription, translation, and minimal metabolism. The members of the proteome core seem to be tightly interconnected with a number of interactions forming core interactome whether or not additional species-specific proteins are located on the periphery. We also obtained a genome core of the respective organisms and compared it with the proteome core. It was found that the genome core encodes 73 more proteins than the proteome core. Apart of proteins which may not be identified due to technical limitations, there are 24 proteins that seem to not be expressed under the optimal conditions.

Show MeSH
Related in: MedlinePlus