Home LiteratureArticle Details
PMID: 4922293 Published · ppublish English Journal Article

DNA ligase mutants of Escherichia coli.

Gellert M, Bullock ML

Abstract

A procedure is described for the isolation of Escherichia coli mutants with either excess or deficient DNA ligase activity. A mutant that overproduces DNA ligase supports the growth of ligase-defective (gene 30 mutant) T4 phages. Even T4 rII-gene 30 double mutants, which are able to grow in normal E. coli, cannot grow in cells deficient in DNA ligase. A functional DNA ligase, supplied either by the phage or the host, thus seems to be required for T4 growth. An E. coli strain that makes a temperature-sensitive DNA ligase becomes radiation-sensitive at high temperature, but otherwise grows normally and shows no obvious defect in DNA replication.

MeSH Terms
Centrifugation, Density Gradient DNA, Bacterial Escherichia coli/enzymology Genetics, Microbial Ligases/metabolism Mutation Temperature
Chemicals
DNA, Bacterial Ligases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gellert M
Bullock M L
References (27)
27 references, click to expand
  1. Cohesive sites on the deoxyribonucleic acids from several temperate coliphages.
    J Mol Biol. 1966 Jun;17(2):343-57 PMID: 5336321
  2. Enzymatic breakage and joining of deoxyribonucleic acid, I. Repair of single-strand breaks in DNA by an enzyme system from Escherichia coli infected with T4 bacteriophage.
    Proc Natl Acad Sci U S A. 1967 Apr;57(4):1021-8 PMID: 5340583
  3. Enzymatic joining of DNA strands: a novel reaction of diphosphopyridine nucleotide.
    Proc Natl Acad Sci U S A. 1967 Jun;57(6):1841-8 PMID: 4291949
  4. Linkage of polynucleotides through phosphodiester bonds by an enzyme from Escherichia coli.
    Proc Natl Acad Sci U S A. 1967 May;57(5):1426-33 PMID: 5341238
  5. Formation of covalent circles of lambda DNA by E. coli extracts.
    Proc Natl Acad Sci U S A. 1967 Jan;57(1):148-55 PMID: 4860192
  6. Enzymatic breakage and joining of deoxyribonucleic acid. II. The structural gene for polynucleotide ligase in bacteriophage T4.
    Proc Natl Acad Sci U S A. 1967 Aug;58(2):665-72 PMID: 5234326
  7. Mechanism of DNA chain growth. I. Possible discontinuity and unusual secondary structure of newly synthesized chains.
    Proc Natl Acad Sci U S A. 1968 Feb;59(2):598-605 PMID: 4967086
  8. Role of polynucleotide ligase in T4 DNA replication.
    J Mol Biol. 1968 Aug 14;35(3):639-42 PMID: 4877007
  9. Mechanism of DNA chain growth, II. Accumulation of newly synthesized short chains in E. coli infected with ligase-defective T4 phages.
    Proc Natl Acad Sci U S A. 1968 Aug;60(4):1356-62 PMID: 4299945
  10. Properties of a temperature-sensitive radiation-sensitive mutant of Escherichia coli.
    Proc Natl Acad Sci U S A. 1968 Aug;60(4):1495-502 PMID: 4877274
  11. DNA replication in vivo by a temperature-sensitive polynucleotide ligase mutant of T4.
    Proc Natl Acad Sci U S A. 1968 Nov;61(3):997-1004 PMID: 5246564
  12. Enzymatic synthesis of deoxyribonucleic acid. XXVI. Physical and chemical studies of a homogeneous deoxyribonucleic acid polymerase.
    J Biol Chem. 1969 Jun 10;244(11):2996-3008 PMID: 4890762
  13. Studies on the joining of DNA by polynucleotide ligase of phage T4.
    Cold Spring Harb Symp Quant Biol. 1968;33:151-64 PMID: 4891960
  14. Joining of DNA strands by DNA ligase of E. coli.
    Cold Spring Harb Symp Quant Biol. 1968;33:21-6 PMID: 4306814
  15. Role of polynucleotide ligase and DNA polymerase in the repair of DNA damage.
    J Mol Biol. 1969 Jun 14;42(2):375-8 PMID: 4896027
  16. Enzymatic joining of deoxyribonucleic acid strands. 3. Further purification of the deoxyribonucleic acid ligase from Escherichia coli and multiple forms of the purified enzyme.
    J Biol Chem. 1969 Sep 10;244(17):4689-95 PMID: 4897246
  17. DNA replication of phage T4 rII mutants without polynucleotide ligase (gene 30).
    Biochem Biophys Res Commun. 1969 Oct 22;37(3):416-22 PMID: 4900136
  18. Duplicate genes for tyrosine transfer RNA in Escherichia coli.
    J Mol Biol. 1970 Jan 14;47(1):1-13 PMID: 4905086
  19. Suppression of T4D ligase mutations by rIIa and rIIb mutations.
    Proc Natl Acad Sci U S A. 1969 Nov;64(3):897-904 PMID: 5264148
  20. Intergenic suppression of amber polynucleotide ligase mutation in bacteriophage T4.
    Virology. 1970 Feb;40(2):403-6 PMID: 4909415
  21. Properties of a temperature-sensitive, radiation-sensitive mutant of Escherichia coli. II. DNA replication.
    Proc Natl Acad Sci U S A. 1969 Dec;64(4):1195-202 PMID: 4916921
  22. Enzymatic joining of polynucleotides. IX. A simple and rapid assay of polynucleotide joining (ligase) activity by measurement of circle formation from linear deoxyadenylate-deoxythymidylate copolymer.
    J Biol Chem. 1970 Jul 25;245(14):3626-31 PMID: 4919213
  23. Transduction and segregation in Escherichia coli K12.
    Virology. 1957 Oct;4(2):366-84 PMID: 13496552
  24. Chromosome brekage accompanying genetic recombination in bacteriophage.
    Proc Natl Acad Sci U S A. 1961 Jun 15;47:857-68 PMID: 13769766
  25. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI.
    J Biol Chem. 1964 Jan;239:222-32 PMID: 14114848
  26. CHROMOSOME STRUCTURE IN PHAGE T4. I. CIRCULARITY OF THE LINKAGE MAP.
    Proc Natl Acad Sci U S A. 1964 May;51:775-9 PMID: 14172990
  27. RELEASE OF ULTRAVIOLET LIGHT-INDUCED THYMINE DIMERS FROM DNA IN E. COLI K-12.
    Proc Natl Acad Sci U S A. 1964 Feb;51:293-300 PMID: 14124327
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1970-11-00
Pages
1580-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC283393
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]