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LAMBD:HOLIN
Contents
| Species (Taxon ID) | Escherichia phage lambda (Bacteriophage lambda). (10710) | |
| Gene Name(s) | S | |
| Protein Name(s) | Antiholin (ECO:0000303 with PMID:8878031[1])
Lysis inhibitor S-107 (ECO:0000303 with PMID:8878031[1]) Holin (ECO:0000303 with PMID:8878031[1]) Lysis protein S-105 (ECO:0000303 with PMID:8878031[1]) gpS protein | |
| External Links | ||
| UniProt | P03705 | |
| EMBL | J02459 M14035 | |
| PIR | H94164 | |
| RefSeq | NP_040644.1 YP_001551775.1 | |
| IntAct | P03705 | |
| TCDB | 1.E.2.1.1 | |
| GeneID | 2703479 5740919 | |
| KEGG | vg:2703479 vg:5740919 | |
| OrthoDB | VOG090001HJ | |
| Proteomes | UP000001711 | |
| GO | GO:0020002 GO:0016021 GO:0034291 | |
| InterPro | IPR006481 | |
| Pfam | PF05106 | |
| TIGRFAMs | TIGR01594 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0020002 |
host cell plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
In Figure 4e. a 15,00 molecular weight protein was present in the fraction corresponding to the inner membrane, and was not present in S- cells. |
complete | ||||
| GO:0034291 |
canonical holin activity |
ECO:0000315 |
F |
Figure 2A. Shows a deletion of S fails to yield induction of lysis in the host. The figure also shows the presence of S restores this activity. Paper states S is a holin. |
complete | |||||
| GO:0046983 |
protein dimerization activity |
ECO:0000314 |
F |
Figure 2A. Shows Lambda Holin "S105" can dimerize. |
complete | |||||
| GO:0020002 |
host cell plasma membrane |
ECO:0000314 |
C |
Figure 3. shows dimer formation in the membrane. In methods - "soluble fractions of inner membrane proteins were prepared" |
complete | |||||
| GO:0051259 |
protein oligomerization |
ECO:0000314 |
P |
Figure 7. Gel shows Lambda S can oligomerize. |
complete | |||||
| GO:0020002 |
host cell plasma membrane |
ECO:0000314 |
C |
Figure 7. shows cross-linking of membrane proteins. mentions twice in paper -"preferential extraction of inner membrane proteins with Triton X-100" |
complete | |||||
| GO:0020002 |
host cell plasma membrane |
ECO:0000315 |
C |
Figure 1: Lysis requires the genes S and R. R codes for endolysin. S codes for the holin and holin inhibitor (genes 105 and 107) in Lambda. Lambda phages were mutated to be either without the holin gene (S), and with the endolysin (R) gene (or vice versa) or with both holin and endolysin gene. And as seen in the image, the lambda phages without the S gene did not lyse. However, the lambda phages with out R did lyse, at about 60 minuets. And the Lambda phage with both lysed at 40 minuets, which was the quickest lyse without the help of methyl trichloride. This suggests that endolysin is not required for lysis but involved in cleaving the bonds in the peptidoglycan. |
complete | |||||
| GO:0045918 |
negative regulation of cytolysis |
ECO:0000314 |
P |
Figure 3. S105, holin, and S107, antiholin, are two transmembrane proteins produced by alternate starts on gene S in phage lambda. S105 accumulates into rafts, which are associated with the formation of large holes in the membrane. These holes allow endolysin to reach the peptidoglycan and result in cytolysis. S105 has three transmembrane domains. The difference between S105 and S107 is an extra N-terminal positive charge on S107, which prevents the first transmembrane domain from entering the membrane. The researchers created a mutant allele of S105 with the first transmembrane domain deleted, such that it would act like S107, and fused it to mCherryFP. Through deconvolution fluorescence imaging, they showed that the fusion protein blocked S105 raft formation, suggesting that antiholins prevent lysis by blocking the formation of holin rafts. |
complete | |||||
|
involved_in |
GO:0044659 |
cytolysis by virus of host cell |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0020002 |
host cell plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0020002 |
host cell plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0034291 |
canonical holin activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0020002 |
host cell plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0044660 |
cytolysis by virus via pore formation in host cell membrane |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0034291 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0033644 |
host cell membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0020002 |
host cell plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-1030 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019835 |
cytolysis |
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.
- ↑ 1.0 1.1 1.2 1.3 Bläsi, U & Young, R (1996) Two beginnings for a single purpose: the dual-start holins in the regulation of phage lysis. Mol. Microbiol. 21 675-82 PubMed GONUTS page
- ↑ 2.0 2.1 Wilson, DB (1982) Effect of the lambda S gene product on properties of the Escherichia coli inner membrane. J. Bacteriol. 151 1403-10 PubMed GONUTS page
- ↑ 3.0 3.1 Ramanculov, E & Young, R (2001) Functional analysis of the phage T4 holin in a lambda context. Mol. Genet. Genomics 265 345-53 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Gründling, A et al. (2000) Dimerization between the holin and holin inhibitor of phage lambda. J. Bacteriol. 182 6075-81 PubMed GONUTS page
- ↑ 5.0 5.1 5.2 Zagotta, MT & Wilson, DB (1990) Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli. J. Bacteriol. 172 912-21 PubMed GONUTS page
- ↑ Wang, IN et al. (2000) Holins: the protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54 799-825 PubMed GONUTS page
- ↑ White, R et al. (2011) Holin triggering in real time. Proc. Natl. Acad. Sci. U.S.A. 108 798-803 PubMed GONUTS page
- ↑ Smith, DL et al. (1998) Purification and biochemical characterization of the lambda holin. J. Bacteriol. 180 2531-40 PubMed GONUTS page
