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Gene Review

lys  -  lysis protein

Enterobacteria phage MS2

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Disease relevance of MS2g3


High impact information on MS2g3

  • Overlapping genes in RNA phage: a new protein implicated in lysis [3].
  • The mutations, which are clustered ahead of the overlapping lysis cistron, do not change the amino acid sequence of the coat protein, but they disrupt a local hairpin, which is needed to control translation of the lysis gene [4].
  • We assume that the ribosome, terminating at the coat reading frame, covers part of the lysis hairpin, thereby destabilizing the secondary structure [5].
  • Activation of the L gene is suppressed when the stability of the lysis initiator hairpin is increased by mutations that create additional base-pairs [5].
  • Deletions or point mutations that are predicted to destabilize the hairpin give rise to lysis protein synthesis that is independent of coat gene translation [6].

Chemical compound and disease context of MS2g3


Biological context of MS2g3


Anatomical context of MS2g3


Associations of MS2g3 with chemical compounds

  • After extensive separation of the membranes by isopycnic sucrose gradient centrifugation, the lysis protein was present predominantly in the cytoplasmic membrane and in a fraction of intermediate density and, to a lesser degree, in the outer membrane, irrespective of the conditions of growth [10].
  • No change in the capacity of the binding proteins to bind 14C-labelled penicillin G was observed in the presence of the MS2 lysis gene product [7].


  1. Lysis gene expression of RNA phage MS2 depends on a frameshift during translation of the overlapping coat protein gene. Kastelein, R.A., Remaut, E., Fiers, W., van Duin, J. Nature (1982) [Pubmed]
  2. Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping gene encoding a lysis function. Atkins, J.F., Steitz, J.A., Anderson, C.W., Model, P. Cell (1979) [Pubmed]
  3. Overlapping genes in RNA phage: a new protein implicated in lysis. Beremand, M.N., Blumenthal, T. Cell (1979) [Pubmed]
  4. Rapid evolution of translational control mechanisms in RNA genomes. Klovins, J., Tsareva, N.A., de Smit, M.H., Berzins, V., van Duin, J. J. Mol. Biol. (1997) [Pubmed]
  5. Lysis gene of bacteriophage MS2 is activated by translation termination at the overlapping coat gene. Berkhout, B., Schmidt, B.F., van Strien, A., van Boom, J., van Westrenen, J., van Duin, J. J. Mol. Biol. (1987) [Pubmed]
  6. Determination of the RNA secondary structure that regulates lysis gene expression in bacteriophage MS2. Schmidt, B.F., Berkhout, B., Overbeek, G.P., van Strien, A., van Duin, J. J. Mol. Biol. (1987) [Pubmed]
  7. Functioning of the cloned phage MS2 lysis protein in Escherichia coli impaired in murein synthesis. Ursinus-Wössner, A., Höltje, J.V. FEMS Microbiol. Lett. (1989) [Pubmed]
  8. Specific localization of the lysis protein of bacteriophage MS2 in membrane adhesion sites of Escherichia coli. Walderich, B., Höltje, J.V. J. Bacteriol. (1989) [Pubmed]
  9. Nucleotide sequence from the ssRNA bacteriophage JP34 resolves the discrepancy between serological and biophysical classification. Adhin, M.R., Hirashima, A., van Duin, J. Virology (1989) [Pubmed]
  10. Induction of the autolytic system of Escherichia coli by specific insertion of bacteriophage MS2 lysis protein into the bacterial cell envelope. Walderich, B., Ursinus-Wössner, A., van Duin, J., Höltje, J.V. J. Bacteriol. (1988) [Pubmed]
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