The mode of inhibitory action by pyridoxal 5-phosphate on DNA polymerase-α and -β | Zendy

Mieko Oguro | Zendy; Hiroshi Nagano | Zendy; Yoshitake Mano | Zendy

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The mode of inhibitory action by pyridoxal 5-phosphate on DNA polymerase-α and -β

Author(s) -

Mieko Oguro,

Hiroshi Nagano,

Yoshitake Mano

Publication year - 1979

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/7.3.727

Subject(s) - dna polymerase , primer (cosmetics) , biology , microbiology and biotechnology , dna clamp , dna polymerase ii , biochemistry , polymerase , dna , dna polymerase beta , dna polymerase i , non competitive inhibition , pyridoxal , pyridoxal phosphate , primase , phosphate , enzyme , dna repair , chemistry , polymerase chain reaction , reverse transcriptase , gene , base excision repair , organic chemistry , cofactor

The kinetics of the inhibition of DNA polymerases-alpha and -beta from sea urchin embryos by pyridoxal 5-phosphate were studied. The inhibition of DNA polymerase-alpha activity by pyridoxal 5-phosphate was competitive with activated DNA but noncompetitive with each deoxynucleoside triphosphate. With poly(dC)-oligo(dG)12-18 as a template-primer, however, the inhibition of DNA polymerase-alpha was competitive with dGTP but noncompetitive with the template-primer. These results suggest that DNA polymerase-alpha interacts with activated DNA and poly(dC)-oligo(dG)12-18 in different ways. The inhibition of DNA polymerase-beta by pyridoxal 5-phosphate was competitive with deoxynucleoside triphosphate using activated DNA as a template-primer and noncompetitive with activated DNA. Using poly(rA)-oligo(dT)12-18 as a template-primer, DNA polymerase-beta activity yielded sigmoid curves against both dTTP and the template-primer concentrations and was inhibited by pyridoxal 5-phosphate noncompetitively with respect to both dTTP and the template-primer. These results indicate that the inhibitory mode of DNA polymerase-alpha by pyridoxal 5-phosphate is different from that of DNA polymerase-beta.

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