Abstract
Bacterial mutants have been isolated, called groN, that block phage development by interference with the action of the product of the phage N gene. lambdatrp phages, which depend on the N product for the synthesis of tryptophan enzymes, do not make these enzymes in groN bacteria. Two type of phage mutants have been isolated that can overcome the groN block. One type makes an altered N product, the other contains an N-bypass mutation. The groN mutation is closely linked to the rifamycin-resistance locus in Escherichia coli. Purified RNA polymerase from the groN mutant is less activated by salt and more sensitive to rifamycin than is the polymerase from gro(+). This suggests that the groN mutation produces a structural change in the bacterial RNA polymerase such that it can no longer interact properly with the phage N product.
MeSH Terms
Bacterial Proteins/metabolism
Bacteriophages/enzymology,metabolism
Binding Sites
Culture Media
Escherichia coli/drug effects,enzymology,metabolism
Genetic Code
Mutation
Operon
Potassium Chloride/pharmacology
Protein Conformation
RNA Nucleotidyltransferases/antagonists & inhibitors,metabolism
RNA, Bacterial/metabolism
Rifampin/pharmacology
Suppression, Genetic
Tryptophan/biosynthesis
Chemicals
Bacterial Proteins
Culture Media
RNA, Bacterial
Potassium Chloride
Tryptophan
RNA Nucleotidyltransferases
Rifampin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Georgopoulos C P
References (17)
17 references, click to expand
-
Genetic studies on bacteriophage P1.
Virology. 1968 Dec;36(4):564-74
PMID: 4881411
-
Studies of novel transducing variants of lambda: dispensability of genes N and Q.
Virology. 1969 Oct;39(2):348-52
PMID: 5344297
-
Termination factor for RNA synthesis.
Nature. 1969 Dec 20;224(5225):1168-74
PMID: 4902144
-
Induction of a new RNA polymerase in Escherichia coli infected with bacteriophage T3.
Biochem Biophys Res Commun. 1971 Apr 16;43(2):443-50
PMID: 4930861
-
On the chemical nature of alteration and modification of DNA dependent RNA polymerase of E. coli after T4 infection.
FEBS Lett. 1971 Aug 15;16(3):175-179
PMID: 11945932
-
Orientation and control of transcription in E. coli phage lambda.
Nature. 1969 Mar 1;221(5183):823-5
PMID: 5765054
-
Regulation of repressor expression in lambda.
Proc Natl Acad Sci U S A. 1970 Jul;66(3):855-62
PMID: 5269249
-
Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits.
J Bacteriol. 1969 Feb;97(2):734-42
PMID: 4886290
-
Structural alteration of RNA polymerase during sporulation.
Nature. 1970 Aug 29;227(5261):910-3
PMID: 4988657
-
A bacterial mutation which affects recognition of the N gene product of bacteriophage lambda.
Mol Gen Genet. 1970;108(4):374-5
PMID: 4924699
-
Location of the phage lambda gene responsible for turning off lambda-exonuclease synthesis.
Virology. 1970 Jan;40(1):65-71
PMID: 5411194
-
Two states of expression of genes cl, rex, and N in lambda.
Virology. 1971 Jan;43(1):16-33
PMID: 5543270
-
Studies of the messenger RNA of bacteriophage lambda, I. Various species synthesized early after induction of the prophage.
Proc Natl Acad Sci U S A. 1968 Nov;61(3):1013-20
PMID: 5246538
-
Relationships between bactericidal effect and inhibition of ribonucleic acid nucleotidyltransferase by rifampicin in Escherichia coli K-12.
J Bacteriol. 1969 Feb;97(2):761-8
PMID: 4886292
-
New RNA polymerase from Escherichia coli infected with bacteriophage T7.
Nature. 1970 Oct 17;228(5268):227-31
PMID: 4920917
-
Deletion mapping of the c-3-N region of bacteriophage.
Virology. 1969 Sep;39(1):137-41
PMID: 5812352
-
A rifampicin resistent rna-polymerase from E. coli altered in the beta-subunit.
FEBS Lett. 1969 Oct 21;5(2):104-106
PMID: 11947251