Back to Search
Start Over
Phi X174 lysis requires slyD, a host gene which is related to the FKBP family of peptidyl-prolyl cis-trans isomerases.
- Source :
-
FEMS microbiology reviews [FEMS Microbiol Rev] 1995 Aug; Vol. 17 (1-2), pp. 213-8. - Publication Year :
- 1995
-
Abstract
- Recessive mutations in the slyD (sensitivity to lysis) gene were isolated by selecting for survival after induction of the cloned lysis gene E of bacteriophage phi X174 [1]. The slyD- mutation, transduced into the normal phi X174 host, Escherichia coli C, confers an absolute block on the plaque-forming ability of the wild-type phage, indicating that slyD is required for E function. slyD encodes a protein with 196 residues. A segment corresponding to the first 142 residues of the predicted SlyD protein has significant similarity throughout its length to the FKBP family of peptidyl-prolyl cis-trans isomerases, or rotamases. The C-terminal 46 codons of slyD encode a remarkable histidine-rich peptide which is a metal-binding domain [2]. This sequence is dispensable for slyD function in E-mediated lysis. Although there is no obvious phenotype associated with the slyD- genotype other than the resistance to E-mediated lysis, overexpression of slyD causes cells to filament and to increase significantly in diameter. Mutations in phi X174 can restore the plaque-forming ability of the phage on a slyD- host. These pos (plates on slyD) mutants plate on E. coli C wild-type and slyD-. A model for SlyD involvement in E function and the role of SlyD in the cell is discussed.
- Subjects :
- Amino Acid Sequence
Binding Sites
Carrier Proteins chemistry
Chromosome Mapping
DNA-Binding Proteins chemistry
Heat-Shock Proteins chemistry
Metals metabolism
Molecular Sequence Data
Peptidylprolyl Isomerase
Tacrolimus Binding Proteins
Amino Acid Isomerases genetics
Bacteriolysis
Bacteriophage phi X 174 physiology
Carrier Proteins genetics
Escherichia coli Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 0168-6445
- Volume :
- 17
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- FEMS microbiology reviews
- Publication Type :
- Academic Journal
- Accession number :
- 7669348
- Full Text :
- https://doi.org/10.1111/j.1574-6976.1995.tb00204.x