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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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Related in: MedlinePlus

Complexes in the proteome core based on M. pneumonia data.Proteins that do not form complexes (35 proteins) are shown on the left. Proteins that are found in complexes (140 proteins) are shown on the right. Color indicates COG functional category (1 sector per protein). Only the most representative complexes are shown. The key for COG functional categories letter code: C Energy production and conversion. D Cell cycle control, cell division, chromosome partitioning. F Nucleotide transport and metabolism. G Carbohydrate transport and metabolism. H Coenzyme transport and metabolism. J Translation, ribosomal structure and biogenesis. K Transcription. L Replication, recombination and repair. O Posttranslational modification, protein turnover, chaperones. P Inorganic ion transport and metabolism. R General function prediction only. U Intracellular trafficking, secretion, and vesicular transport.
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pone-0021964-g004: Complexes in the proteome core based on M. pneumonia data.Proteins that do not form complexes (35 proteins) are shown on the left. Proteins that are found in complexes (140 proteins) are shown on the right. Color indicates COG functional category (1 sector per protein). Only the most representative complexes are shown. The key for COG functional categories letter code: C Energy production and conversion. D Cell cycle control, cell division, chromosome partitioning. F Nucleotide transport and metabolism. G Carbohydrate transport and metabolism. H Coenzyme transport and metabolism. J Translation, ribosomal structure and biogenesis. K Transcription. L Replication, recombination and repair. O Posttranslational modification, protein turnover, chaperones. P Inorganic ion transport and metabolism. R General function prediction only. U Intracellular trafficking, secretion, and vesicular transport.

Mentions: We estimated a possible interaction that may be found in the proteome core based on Mycoplasma pneumonia interactome data [22]. According to M. pneumonia data, most of the COGs in the proteome core (140 COGs) are associated in complexes (Fig 4, Supplementary Table S2). Moreover, 54 COGs participate in more than one complex. Most of the COGs that do not form complexes are ribosomal proteins that are absent in M. pneumonia, are transport COGs, or are unknown proteins (Supplementary Table S3).


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)

Complexes in the proteome core based on M. pneumonia data.Proteins that do not form complexes (35 proteins) are shown on the left. Proteins that are found in complexes (140 proteins) are shown on the right. Color indicates COG functional category (1 sector per protein). Only the most representative complexes are shown. The key for COG functional categories letter code: C Energy production and conversion. D Cell cycle control, cell division, chromosome partitioning. F Nucleotide transport and metabolism. G Carbohydrate transport and metabolism. H Coenzyme transport and metabolism. J Translation, ribosomal structure and biogenesis. K Transcription. L Replication, recombination and repair. O Posttranslational modification, protein turnover, chaperones. P Inorganic ion transport and metabolism. R General function prediction only. U Intracellular trafficking, secretion, and vesicular transport.
© Copyright Policy
Related In: Results  -  Collection

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

pone-0021964-g004: Complexes in the proteome core based on M. pneumonia data.Proteins that do not form complexes (35 proteins) are shown on the left. Proteins that are found in complexes (140 proteins) are shown on the right. Color indicates COG functional category (1 sector per protein). Only the most representative complexes are shown. The key for COG functional categories letter code: C Energy production and conversion. D Cell cycle control, cell division, chromosome partitioning. F Nucleotide transport and metabolism. G Carbohydrate transport and metabolism. H Coenzyme transport and metabolism. J Translation, ribosomal structure and biogenesis. K Transcription. L Replication, recombination and repair. O Posttranslational modification, protein turnover, chaperones. P Inorganic ion transport and metabolism. R General function prediction only. U Intracellular trafficking, secretion, and vesicular transport.
Mentions: We estimated a possible interaction that may be found in the proteome core based on Mycoplasma pneumonia interactome data [22]. According to M. pneumonia data, most of the COGs in the proteome core (140 COGs) are associated in complexes (Fig 4, Supplementary Table S2). Moreover, 54 COGs participate in more than one complex. Most of the COGs that do not form complexes are ribosomal proteins that are absent in M. pneumonia, are transport COGs, or are unknown proteins (Supplementary Table S3).

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