Open AccessThe Escherichia coli heat shock response and bacteriophage λ development
Author(s) -
Polissi Alessandra,
Goffin Laurence,
Georgopoulos Costa
Publication year - 1995
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.1995.tb00198.x
Subject(s) - groel , groes , biology , bacteriophage , lytic cycle , escherichia coli , lysogenic cycle , chaperonin , chaperone (clinical) , heat shock protein , mutant , heat shock , cold shock domain , genetics , microbiology and biotechnology , protein folding , gene , rna , medicine , virus , pathology
The Escherichia coli /bacteriophage λ genetic interaction system has been used to uncover the existence of various biological machines. The starting point of all these studies was the isolation and characterization of E. coli mutants that blocked λ growth, and the corresponding λ compensatory mutations. In this manner, the λN‐promoted transcriptional anti‐termination machine was discovered composed of the NusA/NusB/NusE/NusG host proteins. In addition, the DnaK and GroEL chaperone machines were discovered composed of DnaK/DnaJ/GrpE and GroES/GroEL heat shock proteins. The individual members of the DnaK and GroEL chaperone machines have been conserved throughout evolution in both function and structure. Their biological roles include a direct involvement in λ DNA replication and morphogenesis, the protection of proteins from aggregation, the disaggregation of various protein aggregates, the manipulation of protein structure and function, as well as the autoregulation of the heat shock response. The evolution of λ to extensively rely on the status of the heat shock response of E. coli is likely linked to its lytic versus lysogenic choice of lifestyle. The bacteriophage T4 gp31 protein has been purified and shown to substitute for many of GroES' co‐chaperonin activities.