Difference between revisions of "SubtInteract"
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=== [[cell division]]: the [[divisome]]=== | === [[cell division]]: the [[divisome]]=== | ||
| − | ==Complexes in [[ | + | == Complexes in [[metabolism]], [[ATP synthesis]] and [[respiration]] == |
=== the metabolons of glycolysis and the TCA cycle {{PubMed|19193632,20933603}}=== | === the metabolons of glycolysis and the TCA cycle {{PubMed|19193632,20933603}}=== | ||
| + | === the [[ATP synthase]] === | ||
| + | === [[respiratory complexes and supercomplexes]] === | ||
==Complexes in [[Information processing]]== | ==Complexes in [[Information processing]]== | ||
Revision as of 17:08, 11 August 2013
Protein-protein interactions are essential for many activities of any living cell. These interactions involve multi-protein complexes that take part in central processes such as DNA replication, transcription or translation. Protein-protein interactions may also be involved in a variety of regulatory events. Metabolic enzymes do often form transien complexes that represent a complete pathways. These complexes are called metabolon. Finally, many interactions may be of a transient nature.
Now online: A description of SubtiWiki, SubtiPathways, and SubtInteract in the 2012 Database issue of Nucleic Acids Research
Ulrike Mäder, Arne G Schmeisky, Lope A Flórez, Jörg Stülke
SubtiWiki--a comprehensive community resource for the model organism Bacillus subtilis.
Nucleic Acids Res: 2012, 40(Database issue);D1278-87
[PubMed:22096228]
[WorldCat.org]
[DOI]
(I p)
Contents
- 1 Methods to detect protein-protein interactions
- 2 Visualization of protein-protein interactions in B. subtilis
- 3 Protein complexes in B. subtilis
- 3.1 Complexes in Cellular processes
- 3.2 Complexes in metabolism, ATP synthesis and respiration
- 3.3 Complexes in Information processing
- 3.3.1 Initiation of DNA replication: the primosome
- 3.3.2 DNA replication: the replisome
- 3.3.3 transcription: RNA polymerase
- 3.3.4 translation: the ribosome
- 3.3.5 synthesis of glutamyl-tRNA(Gln): the transamidosome (GatA-GatB-GatC)-GltX-trnS-Gln
- 3.3.6 RNA processing and degradation: the RNA degradosome
- 3.3.7 protein secretion: the signal recognition particle
- 3.4 Complexes involved in Lifestyles
- 4 Suspected hub proteins potentially involved in a large number of interactions (as deduced from a Yeast two-hybrid analysis)
- 5 Important publications
Methods to detect protein-protein interactions
- Yeast Two Hybrid System PubMed
- TAP-Tag purification PubMed
Attention: Each technique detects only about 33% of all interactions PubMed
Visualization of protein-protein interactions in B. subtilis
- interactive protein-protein interaction map
- the beta version of SubtInteract
Protein complexes in B. subtilis
Complexes in Cellular processes
cell wall synthesis and cell shape: the cell wall biosynthetic complex
cell division: the divisome
Complexes in metabolism, ATP synthesis and respiration
the metabolons of glycolysis and the TCA cycle PubMed
the ATP synthase
respiratory complexes and supercomplexes
Complexes in Information processing
Initiation of DNA replication: the primosome
DNA replication: the replisome
transcription: RNA polymerase
translation: the ribosome
synthesis of glutamyl-tRNA(Gln): the transamidosome (GatA-GatB-GatC)-GltX-trnS-Gln
RNA processing and degradation: the RNA degradosome
protein secretion: the signal recognition particle
Complexes involved in Lifestyles
general stress response: the stressosome
DNA uptake: the pseudopilus PubMed
spore germination: the germinosome
Suspected hub proteins potentially involved in a large number of interactions (as deduced from a Yeast two-hybrid analysis)
- FruA, SwrC, XhlA, YhaP, YhgE, YkcC, YqfF, CsbC, CssS, FliZ, MreD, PpsC, RacA, Smc, YclI, YdeL, YdgH, YdbI, YesS, YkoT, YopZ, YqbD, YtdP, YueB, YwqJ, YyxA
Elodie Marchadier, Rut Carballido-López, Sophie Brinster, Céline Fabret, Peggy Mervelet, Philippe Bessières, Marie-Françoise Noirot-Gros, Vincent Fromion, Philippe Noirot
An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach.
Proteomics: 2011, 11(15);2981-91
[PubMed:21630458]
[WorldCat.org]
[DOI]
(I p)
Important publications
