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Maize replicative α‐type DNA polymerase: separation of polymerase and primase activities and recognition of primase subunits
Author(s) -
García Elpidio,
Laquel Patricia,
Castroviejo Michel,
Plasencia Javier,
VázquezRamos Jorge M.
Publication year - 2002
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.2002.1140405.x
Subject(s) - primase , dna polymerase , dna clamp , dna polymerase ii , polymerase , biology , microbiology and biotechnology , dna polymerase i , primer (cosmetics) , dna , dna replication , biochemistry , chemistry , polymerase chain reaction , gene , reverse transcriptase , organic chemistry
DNA polymerase and DNA primase activities in the maize α‐type DNA polymerase 2 were dissociated and DNA polymerase‐free DNA primase was studied. DNA primase synthesized primers that were 8–34 nucleotides long, with more intense bands at 15–17 nucleotides in length. DNA polymerase 1 (a putative δ‐type enzyme) or DNA polymerase 2 were assayed after template‐priming with purified DNA primase and showed a differential use of templates: whereas DNA polymerase 2 used a polydT template more efficiently than a natural template, DNA polymerase 1 used both of them poorly. The molecular size of DNA primase was estimated to be 68 kDa by gel filtration, western blotting and by a DNA primase ‘trapping’ assay.