Disease relevance of MS2g3

• Lysis gene expression of RNA phage MS2 depends on a frameshift during translation of the overlapping coat protein gene [1].
• Analysis of the translation products directed by RNA from op3, a UGA nonsense mutant of phage f2, identifies the overlapping cistron as a lysis gene [2].
• We discuss the properties of the overlapping gene in relation to its lysis function, recognition of the lysis initiator region by E. coli versus eucaryotic ribosomes and op3 as a ribosome binding site mutant for the f2 synthetase cistron [2].

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

• In addition, both processes, longitudinal growth of the murein sacculus in the presence of furazlocillin, cephalexin and nalidixic acid as well as spherical growth in the presence of mecillinam were sensitive to the phage lysis protein [7].

Biological context of MS2g3

• Translation of the lysis cistron of MS2 RNA requires a frameshift of ribosomes reading the upstream coat protein mRNA [1].
• The translation of both reading frames is coupled; the synthesis of the lysis protein does not occur unless translation of the overlapping coat gene takes place [5].
• The present findings are also discussed in relation to an earlier proposal for L gene activation [5].
• Polyclonal L-protein-specific antiserum was purified by preabsorption to membranes from cells harboring a control plasmid [8].
• The nucleotide sequence of the coat and lysis genes of the single-stranded RNA bacteriophage JP34 is presented [9].

Anatomical context of MS2g3

• At tolerant conditions, only 21.0% of the L protein was in the adhesion sites; most of the protein (68.2%) was found in inner and outer membranes [8].
• Specific localization of the lysis (L) protein of bacteriophage MS2 in the cell wall of Escherichia coli was determined by immunoelectron microscopy [8].

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].

References