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BPPH2:NP
Contents
| Species (Taxon ID) | Bacillus phage phi29 (Bacteriophage phi-29). (10756) | |
| Gene Name(s) | 6 | |
| Protein Name(s) | Histone-like protein p6 (ECO:0000303 with PMID:12480935[1])
Double-stranded DNA-binding protein p6 (ECO:0000305) Gene product 6 (ECO:0000305) gp6 (ECO:0000305) Nucleoid-associated protein p6 (ECO:0000303 with PMID:12383516[2]) Protein p6 (ECO:0000305) | |
| External Links | ||
| UniProt | P03685 | |
| EMBL | V01154 V01155 EU771092 X04386 | |
| PIR | B92343 | |
| RefSeq | YP_002004534.1 | |
| GeneID | 6446509 | |
| KEGG | vg:6446509 | |
| OrthoDB | VOG090001HF | |
| Proteomes | UP000001207 | |
| GO | GO:0003677 GO:0030261 GO:0006355 GO:0046782 GO:0006351 GO:0039693 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0017053 |
transcriptional repressor complex |
ECO:0000315 |
C |
Figure 1 displays the mutations of protein p4 and their effects on forming the repression complex between proteins p4 and p6 that represses early transcription in Bacillus subtilis phage phi 29. These mutations disallow the formation of a stable complex, hence the repressor complex cannot be formed between proteins p4 and p6 to completely halt early transcription and switch to late transcription. |
complete | |||||
| GO:0006351 |
transcription, DNA-templated |
ECO:0000315 |
P |
The wildtype gel in figure 1 supports transcriptional activity under normal conditions, and it is contrasted and supported by the change in transcription activity recorded in neighboring gels. |
complete | |||||
| GO:0017053 |
transcriptional repressor complex |
ECO:0000315 |
C |
Figure 2B. A DNase I footprinting assay with both the wild type and mutant was run to observe the p6 and p4 complexes with a DNA fragment containing promoters A3, A2b, and A2c. Calles et al. incubated each lane with an increasing concentration of p6 or p4 and observed the footprints, or areas where the DNase fails to cut because of complex bounded onto the DNA. Mutant p4 proteins lead to a decrease in repression due to the failure of the p4-p6 nucleocomplex protein to form, showing the importance of the p4 protein in transcriptional repression. The presence of p4 protein increases the affinity of the p6 protein to bind, which would repress transcription. |
complete | |||||
| GO:0017053 |
transcriptional repressor complex |
ECO:0000314 |
C |
Figure 3. Competitive EMSA with increasing amounts of [p4] and [p6] incubated in each lane to observe the p4-p6 nucleoprotein complex formation at the late A3 promoter between positions -58 to -104. P4 by itself binds downstream of -58 position; P6 by itself binds throughout the -58 to -104 position; suggesting that the p4 protein allows specific sites for the complex to form. |
complete | |||||
| GO:0001217 |
bacterial-type RNA polymerase transcriptional repressor activity, sequence-specific DNA binding |
ECO:0000315 |
F |
In figure 4, RNAP binding to the promoters in phage phi 29 is monitored in the presence of proteins p4 and p6 with or without mutations at the C-end. The gel shows the inability of a stable p4-p6 complex to form in order to properly repress transcription (ie. blocking the binding of RNAP to the A2c promoter), due to a mutation at the C-end of the p4 protein. |
complete | |||||
|
involved_in |
GO:0039693 |
viral DNA genome replication |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003677 |
DNA binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046782 |
regulation of viral transcription |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003677 |
DNA binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006260 |
DNA replication |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003677 |
DNA binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0030261 |
chromosome condensation |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0039693 |
viral DNA genome replication |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Crucitti, P et al. (2003) Bacteriophage phi 29 early protein p17. Self-association and hetero-association with the viral histone-like protein p6. J. Biol. Chem. 278 4906-11 PubMed GONUTS page
- ↑ Abril, A et al. (2002) The in vivo function of phage phi29 nucleoid-associated protein p6 requires formation of dimers. Gene 296 187-94 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 3.4 Calles, B et al. (2002) The phi29 transcriptional regulator contacts the nucleoid protein p6 to organize a repression complex. EMBO J. 21 6185-94 PubMed GONUTS page
- ↑ González-Huici, V et al. (2004) Genome wide, supercoiling-dependent in vivo binding of a viral protein involved in DNA replication and transcriptional control. Nucleic Acids Res. 32 2306-14 PubMed GONUTS page
- ↑ Serrano, M et al. (1990) A novel nucleoprotein complex at a replication origin. Science 248 1012-6 PubMed GONUTS page
- ↑ Camacho, A & Salas, M (2001) Repression of bacteriophage phi 29 early promoter C2 by viral protein p6 is due to impairment of closed complex. J. Biol. Chem. 276 28927-32 PubMed GONUTS page
