scholarly journals Bacteriophage T4 RNA ligase: preparation of a physically homogeneous, nuclease-free enzyme from hyperproducing infected cells

1977 ◽  
Vol 4 (9) ◽  
pp. 3175-3186 ◽  
Author(s):  
N. Patrick Higgins ◽  
Adam P. Geballe ◽  
Thomas J. Snopek ◽  
Akio Sugino ◽  
Nicholas R. Cozzarelli
Keyword(s):  
Bacteriophage T4 ◽  
Free Enzyme ◽  
Rna Ligase ◽  
T4 Rna Ligase ◽  
Infected Cells

scholarly journals RNA Substrate Specificity and Structure-guided Mutational Analysis of Bacteriophage T4 RNA Ligase 2

2004 ◽  
Vol 279 (30) ◽  
pp. 31337-31347 ◽  
Author(s):  
Jayakrishnan Nandakumar ◽  
C. Kiong Ho ◽  
Christopher D. Lima ◽  
Stewart Shuman
Keyword(s):  
Substrate Specificity ◽  
Mutational Analysis ◽  
Bacteriophage T4 ◽  
Rna Ligase ◽  
T4 Rna Ligase

scholarly journals Mutational Analysis of Bacteriophage T4 RNA Ligase 1

2003 ◽  
Vol 278 (32) ◽  
pp. 29454-29462 ◽  
Author(s):  
Li Kai Wang ◽  
C. Kiong Ho ◽  
Yi Pei ◽  
Stewart Shuman
Keyword(s):  
Mutational Analysis ◽  
Bacteriophage T4 ◽  
Rna Ligase ◽  
T4 Rna Ligase

scholarly journals Bacteriophage T4 RNA ligase is gene 63 product, the protein that promotes tail fiber attachment to the baseplate.

1977 ◽  
Vol 74 (8) ◽  
pp. 3355-3359 ◽  
Author(s):  
T. J. Snopek ◽  
W. B. Wood ◽  
M. P. Conley ◽  
P. Chen ◽  
N. R. Cozzarelli
Keyword(s):  
Bacteriophage T4 ◽  
Tail Fiber ◽  
Rna Ligase ◽  
T4 Rna Ligase

scholarly journals Direct comparison of nick-joining activity of the nucleic acid ligases from bacteriophage T4

2006 ◽  
Vol 398 (1) ◽  
pp. 135-144 ◽  
Author(s):  
Desmond R. Bullard ◽  
Richard P. Bowater
Keyword(s):  
Nucleic Acids ◽  
Bacteriophage T4 ◽  
Strand Break ◽  
Ph Optimum ◽  
Systematic Analysis ◽  
Single Strand Break ◽  
T4 Dna Ligase ◽  
Rna Ligase ◽  
Dna And Rna ◽  
T4 Rna Ligase

The genome of bacteriophage T4 encodes three polynucleotide ligases, which seal the backbone of nucleic acids during infection of host bacteria. The T4Dnl (T4 DNA ligase) and two RNA ligases [T4Rnl1 (T4 RNA ligase 1) and T4Rnl2] join a diverse array of substrates, including nicks that are present in double-stranded nucleic acids, albeit with different efficiencies. To unravel the biochemical and functional relationship between these proteins, a systematic analysis of their substrate specificity was performed using recombinant proteins. The ability of each protein to ligate 20 bp double-stranded oligonucleotides containing a single-strand break was determined. Between 4 and 37 °C, all proteins ligated substrates containing various combinations of DNA and RNA. The RNA ligases ligated a more diverse set of substrates than T4Dnl and, generally, T4Rnl1 had 50–1000-fold lower activity than T4Rnl2. In assays using identical conditions, optimal ligation of all substrates was at pH 8 for T4Dnl and T4Rnl1 and pH 7 for T4Rnl2, demonstrating that the protein dictates the pH optimum for ligation. All proteins ligated a substrate containing DNA as the unbroken strand, with the nucleotides at the nick of the broken strand being RNA at the 3′-hydroxy group and DNA at the 5′-phosphate. Since this RNA–DNA hybrid was joined at a similar maximal rate by T4Dnl and T4Rnl2 at 37 °C, we consider the possibility that this could be an unexpected physiological substrate used during some pathways of ‘DNA repair’.

Catalysis of DNA joining by bacteriophage T4 RNA ligase

1976 ◽  
Vol 68 (2) ◽  
pp. 417-424 ◽  
Author(s):  
Thomas J. Snopek ◽  
Akio Sugino ◽  
Kan L. Agarwal ◽  
Nicholas R. Cozzarelli
Keyword(s):  
Bacteriophage T4 ◽  
Rna Ligase ◽  
T4 Rna Ligase
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