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LAMBD:HOLIN

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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

PMID:6213604[2]

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
CACAO 10384

GO:0034291

canonical holin activity

PMID:11361346[3]

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
CACAO 10420

GO:0046983

protein dimerization activity

PMID:11029427[4]

ECO:0000314

F

Figure 2A. Shows Lambda Holin "S105" can dimerize.

complete
CACAO 10445

GO:0020002

host cell plasma membrane

PMID:11029427[4]

ECO:0000314

C

Figure 3. shows dimer formation in the membrane. In methods - "soluble fractions of inner membrane proteins were prepared"

complete
CACAO 10446

GO:0051259

protein oligomerization

PMID:2137120[5]

ECO:0000314

P

Figure 7. Gel shows Lambda S can oligomerize.

complete
CACAO 10447

GO:0020002

host cell plasma membrane

PMID:2137120[5]

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
CACAO 10449

GO:0020002

host cell plasma membrane

PMID:11018145[6]

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
CACAO 12890

GO:0045918

negative regulation of cytolysis

PMID:21187415[7]

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
CACAO 13115

involved_in

GO:0044659

cytolysis by virus of host cell

PMID:9573208[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0020002

host cell plasma membrane

PMID:2137120[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0020002

host cell plasma membrane

PMID:11029427[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0034291

canonical holin activity

PMID:11361346[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0020002

host cell plasma membrane

PMID:6213604[2]

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

GO_REF:0000108

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

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0033644

host cell membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1043

C

Seeded From UniProt

complete

part_of

GO:0020002

host cell plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1030
UniProtKB-KW:KW-1032
UniProtKB-SubCell:SL-0373

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

involved_in

GO:0019835

cytolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0204

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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. 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. 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. 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. 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
  6. Wang, IN et al. (2000) Holins: the protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54 799-825 PubMed GONUTS page
  7. White, R et al. (2011) Holin triggering in real time. Proc. Natl. Acad. Sci. U.S.A. 108 798-803 PubMed GONUTS page
  8. Smith, DL et al. (1998) Purification and biochemical characterization of the lambda holin. J. Bacteriol. 180 2531-40 PubMed GONUTS page