Host participation in bacteriophage lambda head assembly

Georgopoulos, Costa; Hendrix, Roger W.; Casjens, Sherwood; Kaiser, A.D.

doi:10.1016/0022-2836(73)90080-6

Cited by 363 publications

(209 citation statements)

References 28 publications

Supporting

Mentioning

203

Contrasting

Unclassified

Order By: Relevance

“…GroEL was first identified because it is essential for the assembly of bacteriophages (Georgopoulos et al, 1973) ; however it is also essential for growth of E. coli under normal conditions (Fayet et al, 1989). Interestingly mutants of groEL exhibit phenotypes similar to those of the hsp7O-homologue DnaK.…”

Section: Bacterial Hsp6wgroelmentioning

confidence: 99%

Heat‐shock proteins as molecular chaperones

Becker

Craig

1994

European Journal of Biochemistry

488

221

View full text Add to dashboard Cite

Functional proteins within cells are normally present in their native, completely folded form. However, vital processes of protein biogenesis such as protein synthesis and translocation of proteins into intracellular compartments require the protein to exist temporarily in an unfolded or partially folded conformation. As a consequence, regions buried when a polypeptide is in its native conformation become exposed and interact with other proteins causing protein aggregation which is deleterious to the cell. To prevent aggregation as proteins become unfolded, heat‐shock proteins protect these interactive surfaces by binding to them and facilitating the folding of unfolded or nascent polypeptides. In other instances the binding of heat‐shock proteins to interactive surfaces of completely folded proteins is a crucial part of their regulation. As heat shock and other stress conditions cause cellular proteins to become partially unfolded, the ability of heat‐shock proteins to protect cells against the adverse effects of stress becomes a logical extension of their normal function as molecular chaperones.

show abstract

Section: Bacterial Hsp6wgroelmentioning

confidence: 99%

Heat‐shock proteins as molecular chaperones

Becker

Craig

1994

European Journal of Biochemistry

488

221

View full text Add to dashboard Cite

show abstract

“…Thus, although DNA replication is normal, DNA cutting does not occur in cells infected with phage that are mutated in genes involved in procapsid morphogenesis, or in genes D and FI, or in host mutants that block procapsid assembly (Dove, 1966;MacKinley and Kaiser, 1969;Wake et al, 1972;Georgopoulos et al, 1973;Laski and Jackson, 1982;Murialdo et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Mutations of the coat protein gene of bacteriophage λ that overcome the necessity for the FI gene; the EFi domain

Murialdo

Tzamtzis

1997

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe functions of most of the 10 genes involved in phage capsid morphogenesis are well understood. The function of the FI gene is one of the exceptions. Mutants in FI fail to mature and package DNA. The gene product (gpFI) seems to act as a catalyst for the formation of an intermediate in capsid assembly called complex II, which contains a procapsid (an empty capsid precursor), terminase (the enzyme that cleaves the DNA precursor and packages it into the procapsid) and DNA. The mechanism for this stimulation remains unknown. It has also been reported that gpFI appeared to stimulate terminase-mediated cos cleavage, in the absence of procapsids, by increasing enzyme turnover. In comparison with other head-gene mutants, FI mutants are leaky, producing approx. 0.1 phage per infected cell. Some second-site revertants of FI ¹ phages, called 'fin', that bypass the necessity for gpFI, have been isolated and found to harbour a mutation in the genes that code for the two subunits of terminase. In the course of mapping additional fin mutants, it was discovered that some mapped outside the terminase genes. To localize the mutations, restriction fragments of fin mutant DNAs were subcloned into plasmids and their ability to contribute to fin function was determined by marker-rescue analysis. The location of the fin mutation was further delineated by deletion analysis of a plasmid that was positive for fin. This showed that some fin mutations mapped to a region comprising genes E, D and a portion of C. The sequencing of this entire region in several fin isolates showed that the fin mutations are clustered in a small region of gene E corresponding to a portion of 26 amino acid residues of the coat protein (gpE ). We have called this region of the protein the EFi domain.All the mutations result in an increase in positive charge relative to the wild-type protein. These results suggest that DNA maturation and packaging are in part controlled by an interaction between gpFI and capsid gpE.

show abstract

“…One of the partlcularly well studied families of molecular chaperones is the cllaperonins [2,3]. Members of this protein family were first identified in eubacteria (GroEL in Escherichia coli) [4] and in o:rtain organelles of eukaryotic cells, such as mitochondria (I-Isp60 in mitochondrial matrix) [5] and chloroplasts (Rubisc,)-subunit-binding protein, RBP) [6]. These proteins assemble irito large oligomeric complexes of 60 kDa subunits that are usually arranged as two stacked heptameric rings with a central cavity (for review [2,3]).…”

Section: Introductionmentioning

confidence: 99%