Faculty Opinions recommendation of Identification of a specific telomere terminal transferase activity in Tetrahymena extracts.

2012 ◽  
Author(s):  
Neal Young
Keyword(s):  
Transferase Activity ◽  
Terminal Transferase

scholarly journals Identification of a specific telomere terminal transferase activity in tetrahymena extracts

Cell ◽  
1985 ◽  
Vol 43 (2) ◽  
pp. 405-413 ◽  
Author(s):  
Carol W. Greider ◽  
Elizabeth H. Blackburn
Keyword(s):  
Transferase Activity ◽  
Terminal Transferase

scholarly journals Glucocorticoid receptor concentrations and terminal transferase activity as indicators of prognosis in acute non-lymphocytic leukaemia.

BMJ ◽  
1981 ◽  
Vol 282 (6279) ◽  
pp. 1826-1829 ◽  
Author(s):  
L Skoog ◽  
B Nordenskjold ◽  
A Ost ◽  
B Andersson ◽  
R Hast ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Lymphocytic Leukaemia ◽  
Transferase Activity ◽  
Terminal Transferase

Simple and label-free strategy for terminal transferase assay using a personal glucose meter

2020 ◽  
Vol 56 (63) ◽  
pp. 8912-8915
Author(s):  
Hyo Yong Kim ◽  
Jayeon Song ◽  
Ki Soo Park ◽  
Hyun Gyu Park
Keyword(s):  
Glucose Oxidase ◽  
Cerium Oxide ◽  
Cerium Oxide Nanoparticles ◽  
Oxide Nanoparticles ◽  
Transferase Activity ◽  
Label Free ◽  
Activity Assay ◽  
Terminal Transferase ◽  
Personal Glucose Meter ◽  
Glucose Meter

A personal glucose meter-based terminal transferase activity assay utilizing the glucose oxidase-mimicking activity of cerium oxide nanoparticles was developed.

scholarly journals Polymerase θ is a robust terminal transferase that oscillates between three different mechanisms during end-joining

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Tatiana Kent ◽  
Pedro A Mateos-Gomez ◽  
Agnel Sfeir ◽  
Richard T Pomerantz
Keyword(s):  
Terminal Deoxynucleotidyl Transferase ◽  
Transferase Activity ◽  
End Joining ◽  
Switching Mechanism ◽  
Terminal Transferase ◽  
Alternative End Joining ◽  
Nucleotide Insertions ◽  
In Cis

DNA polymerase θ (Polθ) promotes insertion mutations during alternative end-joining (alt-EJ) by an unknown mechanism. Here, we discover that mammalian Polθ transfers nucleotides to the 3’ terminus of DNA during alt-EJ in vitro and in vivo by oscillating between three different modes of terminal transferase activity: non-templated extension, templated extension in cis, and templated extension in trans. This switching mechanism requires manganese as a co-factor for Polθ template-independent activity and allows for random combinations of templated and non-templated nucleotide insertions. We further find that Polθ terminal transferase activity is most efficient on DNA containing 3’ overhangs, is facilitated by an insertion loop and conserved residues that hold the 3’ primer terminus, and is surprisingly more proficient than terminal deoxynucleotidyl transferase. In summary, this report identifies an unprecedented switching mechanism used by Polθ to generate genetic diversity during alt-EJ and characterizes Polθ as among the most proficient terminal transferases known.

scholarly journals Mimivirus encodes a multifunctional primase with DNA/RNA polymerase, terminal transferase and translesion synthesis activities

2019 ◽  
Vol 47 (13) ◽  
pp. 6932-6945 ◽  
Author(s):  
Ankita Gupta ◽  
Shailesh B Lad ◽  
Pratibha P Ghodke ◽  
P I Pradeepkumar ◽  
Kiran Kondabagil
Keyword(s):  
Rna Polymerase ◽  
Reverse Transcriptase ◽  
Biochemical Characterization ◽  
De Novo ◽  
Translesion Synthesis ◽  
Hypothetical Protein ◽  
Protein Product ◽  
Reverse Transcriptase Activity ◽  
Transferase Activity ◽  
Terminal Transferase

Abstract Acanthamoeba polyphaga mimivirus is an amoeba-infecting giant virus with over 1000 genes including several involved in DNA replication and repair. Here, we report the biochemical characterization of gene product 577 (gp577), a hypothetical protein (product of L537 gene) encoded by mimivirus. Sequence analysis and phylogeny suggested gp577 to be a primase-polymerase (PrimPol)—the first PrimPol to be identified in a nucleocytoplasmic large DNA virus (NCLDV). Recombinant gp577 protein purified as a homodimer and exhibited de novo RNA as well as DNA synthesis on circular and linear single-stranded DNA templates. Further, gp577 extends a DNA/RNA primer annealed to a DNA or RNA template using deoxyribonucleoties (dNTPs) or ribonucleotides (NTPs) demonstrating its DNA/RNA polymerase and reverse transcriptase activity. We also show that gp577 possesses terminal transferase activity and is capable of extending ssDNA and dsDNA with NTPs and dNTPs. Mutation of the conserved primase motif residues of gp577 resulted in the loss of primase, polymerase, reverse transcriptase and terminal transferase activities. Additionally, we show that gp577 possesses translesion synthesis (TLS) activity. Mimiviral gp577 represents the first protein from an NCLDV endowed with primase, polymerase, reverse transcriptase, terminal transferase and TLS activities.

scholarly journals Characterization of norovirus 3Dpol RNA-dependent RNA polymerase activity and initiation of RNA synthesis

2006 ◽  
Vol 87 (9) ◽  
pp. 2621-2630 ◽  
Author(s):  
Jacques Rohayem ◽  
Katrin Jäger ◽  
Ivonne Robel ◽  
Ulrike Scheffler ◽  
Achim Temme ◽  
...  
Keyword(s):  
Time Course ◽  
Rna Synthesis ◽  
De Novo ◽  
Polymerase Activity ◽  
Opposite Polarity ◽  
Transferase Activity ◽  
Structural Protein ◽  
Double Stranded Rna ◽  
Terminal Transferase

Norovirus (NV) 3Dpol is a non-structural protein predicted to play an essential role in the replication of the NV genome. In this study, the characteristics of NV 3Dpol activity and initiation of RNA synthesis have been examined in vitro. Recombinant NV 3Dpol, as well as a 3Dpol active-site mutant were expressed in Escherichia coli and purified. NV 3Dpol was able to synthesize RNA in vitro and displayed flexibility with respect to the use of Mg2+ or Mn2+ as a cofactor. NV 3Dpol yielded two different products when incubated with synthetic RNA in vitro: (i) a double-stranded RNA consisting of two single strands of opposite polarity or (ii) the single-stranded RNA template labelled at its 3′ terminus by terminal transferase activity. Initiation of RNA synthesis occurred de novo rather than by back-priming, as evidenced by the fact that the two strands of the double-stranded RNA product could be separated, and by dissociation in time-course analysis of terminal transferase and RNA synthesis activities. In addition, RNA synthesis was not affected by blocking of the 3′ terminus of the RNA template by a chain terminator, sustaining de novo initiation of RNA synthesis. NV 3Dpol displays in vitro properties characteristic of RNA-dependent RNA polymerases, allowing the implementation of this in vitro enzymic assay for the development and validation of antiviral drugs against NV, a so far non-cultivated virus and an important human pathogen.

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