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Nucleic Acids Research, 2002, Vol. 30, No. 23 5056-5064
© 2002 Oxford University Press

Bacillus subtilis {tau} subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P

María I. Martínez-Jiménez, Pablo Mesa and Juan C. Alonso*

Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, C.S.I.C., Campus Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain

*To whom correspondence should be addressed. Tel: +34 91585 4546; Fax: +34 91585 4506; Email: jcalonso{at}cnb.uam.es

Genetic evidence suggests that the Bacillus subtilis dnaX gene only encodes for the {tau} subunit of both DNA polymerases III (Pol IIIs). The B.subtilis full-length protein and their mutant derivatives {tau}(373– 563) (lacking the N-terminal, domains I–III or amino acid residues 1–372) and {tau}(1–372) (lacking the C-terminal region or amino acids 373–563) have been purified. The {tau} protein forms tetramers, {tau}(373– 563) forms dimers, whereas {tau}(1–372), depending on the ionic strength, forms trimers or tetramers in solution. In the absence of single-stranded (ss) DNA and a nucleotide cofactor, {tau} interacts with the SPP1 hexameric replicative G40P DNA helicase in solution or with G40P-ATP bound to ssDNA, with a 1:1 stoichiometry. G40P(109–442), lacking the N-terminal amino acid residues 1–108, interacts with the C-terminal moiety of {tau}. The data indicate that the interaction of G40P with the {tau} subunit of Pol III, is relevant for the loading of the Pol IIIs into the SPP1 G38P-promoted open complex.


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