The characterization and translation in vitro of rabbit globin messenger RNA and messenger ribonucleoprotein labelled with bacteriophage-T4 RNA ligase and 5′-[32P]phosphocytidine 3′-phosphate

1982 ◽  
Vol 10 (2) ◽  
pp. 91-92
Author(s):  
N. SHAUN B. THOMAS ◽  
PHILIP D. BUTCHER ◽  
JOHN M. KELLY ◽  
ROBERT A. COX ◽  
HENRY R. V. ARNSTEIN
Keyword(s):  
Messenger Rna ◽  
Bacteriophage T4 ◽  
Rna Ligase ◽  
Messenger Ribonucleoprotein ◽  
T4 Rna Ligase

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 Transcription of bacteriophage T4 deoxyribonucleic acid in vitro

1969 ◽  
Vol 115 (3) ◽  
pp. 353-361 ◽  
Author(s):  
John O. Bishop ◽  
Forbes W. Robertson
Keyword(s):  
Rna Polymerase ◽  
Messenger Rna ◽  
Rna Synthesis ◽  
Deoxyribonucleic Acid ◽  
Bacteriophage T4 ◽  
Rna Sequences ◽  
Experimental Conditions ◽  
E Coli ◽  
New Methods

1. RNA was synthesized in vitro from a template of bacteriophage T4 DNA, in the presence of Mn2+. A comparison was made of the RNA synthesized by purified RNA polymerase from two sources, Micrococcus lysodeikticus and Escherichia coli; these are referred to as Micrococcus cRNA and E. coli cRNA respectively (where cRNA indicates RNA synthesized in vitro by using purified RNA polymerase and a DNA primer). 2. Both types of RNA were self-complementary as judged by resistance to digestion with ribonuclease after self-annealing, Micrococcus cRNA being more self-complementary (40%) than was E. coli cRNA (30%). The cRNA was found to be much less self-complementary if Mg2+ was present during RNA synthesis instead of Mn2+. 3. Micrococcus cRNA hybridized with a larger part of bacteriophage T4 DNA than did E. coli cRNA. The E. coli cRNA competed with only part (70%) of the Micrococcus cRNA in hybridization-competition experiments. It is concluded that more sequences of bacteriophage T4 DNA are transcribed by Micrococcus polymerase than by E. coli polymerase. 4. The RNA sequences synthesized by Micrococcus RNA polymerase but not by E. coli RNA polymerase are shown by hybridization competition to compete with specifically late bacteriophage T4 messenger RNA sequences. The relevance of this finding to the control of transcription is discussed. 5. In an Appendix, new methods are described for the analysis of hybridization-saturation and -competition experiments. Particular attention is paid to the effects produced if different RNA sequences are present at different relative concentrations. 6. By using cRNA isolated from an enzymically synthesized DNA–RNA hybrid, it is estimated that, of the DNA that is complementary to cRNA, only about half can become hybridized with cRNA under the experimental conditions used.

Synthesis of aspartic acid derivatives useful for the preparation of misacylated transfer RNAs

2000 ◽  
Vol 78 (6) ◽  
pp. 884-891 ◽  
Author(s):  
Michiel Lodder ◽  
Curtis F Crasto ◽  
Andrei L Laikhter ◽  
Haoyun An ◽  
Tuncer Arslan ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Side Chain ◽  
Transfer Rnas ◽  
Rna Ligase ◽  
T4 Rna Ligase ◽  
In Vitro Transcripts ◽  
Derivatives Of

Several derivatives of aspartic acid were protected on Nα as their NVOC derivatives, and on the side chain carboxylates as nitroveratryl esters. Following activation as the cyanomethyl esters, these fully protected aspartate derivatives were converted to the respective pdCpA esters. The protected aspartyl-pdCpA esters were then utilized as substrates for T4 RNA ligase in the presence of in vitro transcripts of tRNA lacking the pCpA dinucleotide normally found at the 3'-end. In this fashion, several misacylated tRNAs were prepared; following photolytic deprotection, these were employed successfully for incorporation into proteins at predetermined positions.Key words: aminoacylated nucleotides, amino acid protection, protein synthesis, tRNA activation.

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
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