The Interaction of Synthetic Templates with Eukaryotic DNA Primase

1995 ◽  
Vol 228 (1) ◽  
pp. 60-67 ◽  
Author(s):  
Rashid O. Anarbaev ◽  
Olga V. Vladimirova ◽  
Olga I. Lavrik
Keyword(s):  
1992 ◽  
Vol 206 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Vladimir N. PODUST ◽  
Olga V. VLADIMIROVA ◽  
Elena N. MANAKOVA ◽  
Olga I. LAVRIK

2000 ◽  
Vol 25 (11) ◽  
pp. 572-576 ◽  
Author(s):  
Bahram Arezi ◽  
Robert D Kuchta
Keyword(s):  

FEBS Letters ◽  
1991 ◽  
Vol 280 (2) ◽  
pp. 281-283 ◽  
Author(s):  
V.N. Podust ◽  
O.V. Vladimirova ◽  
E.N. Manakova ◽  
O.I. Lavrik
Keyword(s):  

1996 ◽  
Vol 119 (6) ◽  
pp. 1038-1044 ◽  
Author(s):  
S. Izuta ◽  
M. Kohsaka-Ichikawa ◽  
T. Yamaguchi ◽  
M. Saneyosh
Keyword(s):  

2021 ◽  
Vol 12 ◽  
Author(s):  
Jan Bergsch ◽  
Jean-Christophe Devillier ◽  
Gunnar Jeschke ◽  
Georg Lipps

Priming of single stranded templates is essential for DNA replication. In recent years, significant progress was made in understanding how DNA primase fulfils this fundamental function, particularly with regard to the initiation. Equally intriguing is the unique property of archeao-eukaryotic primases to terminate primer formation at a well-defined unit length. The apparent ability to “count” the number of bases incorporated prior to primer release is not well understood, different mechanisms having been proposed for different species. We report a mechanistic investigation of primer termination by the pRN1 primase from Sulfolobus islandicus. Using an HPLC-based assay we determined structural features of the primer 5′-end that are required for consistent termination. Mutations within the unstructured linker connecting the catalytic domain to the template binding domain allowed us to assess the effect of altered linker length and flexibility on primer termination.


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