TY - JOUR
T1 - Biochemical evidence of a physical interaction between Sulfolobus solfataricus B-family and Y-family DNA polymerases
AU - De Felice, Mariarita
AU - Medagli, Barbara
AU - Esposito, Luca
AU - De Falco, Mariarosaria
AU - Pucci, Biagio
AU - Rossi, Mosè
AU - Grùz, Petr
AU - Nohmi, Takehiko
AU - Pisani, Francesca M.
PY - 2007/3
Y1 - 2007/3
N2 - The hyper-thermophilic archaeon Sulfolobus solfataricus possesses two functional DNA polymerases belonging to the B-family (Sso DNA pol B1) and to the Y-family (Sso DNA pol Y1). Sso DNA pol B1 recognizes the presence of uracil and hypoxanthine in the template strand and stalls synthesis 3-4 bases upstream of this lesion ("read-ahead" function). On the other hand, Sso DNA pol Y1 is able to synthesize across these and other lesions on the template strand. Herein we report evidence that Sso DNA pol B1 physically interacts with DNA pol Y1 by surface plasmon resonance measurements and immuno-precipitation experiments. The region of DNA pol B1 responsible for this interaction has been mapped in the central portion of the polypeptide chain (from the amino acid residue 482 to 617), which includes an extended protease hyper-sensitive linker between the N- and C-terminal modules (amino acid residues Asn482-Ala497) and the α-helices forming the "fingers" sub-domain (α-helices R, R′ and S). These results have important implications for understanding the polymerase-switching mechanism on the damaged template strand during genome replication in S. solfataricus.
AB - The hyper-thermophilic archaeon Sulfolobus solfataricus possesses two functional DNA polymerases belonging to the B-family (Sso DNA pol B1) and to the Y-family (Sso DNA pol Y1). Sso DNA pol B1 recognizes the presence of uracil and hypoxanthine in the template strand and stalls synthesis 3-4 bases upstream of this lesion ("read-ahead" function). On the other hand, Sso DNA pol Y1 is able to synthesize across these and other lesions on the template strand. Herein we report evidence that Sso DNA pol B1 physically interacts with DNA pol Y1 by surface plasmon resonance measurements and immuno-precipitation experiments. The region of DNA pol B1 responsible for this interaction has been mapped in the central portion of the polypeptide chain (from the amino acid residue 482 to 617), which includes an extended protease hyper-sensitive linker between the N- and C-terminal modules (amino acid residues Asn482-Ala497) and the α-helices forming the "fingers" sub-domain (α-helices R, R′ and S). These results have important implications for understanding the polymerase-switching mechanism on the damaged template strand during genome replication in S. solfataricus.
KW - Archaea
KW - DNA polymerase
KW - DNA replication
KW - Genome stability
KW - Sulfolobus solfataricus
KW - Translesion synthesis
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U2 - 10.1007/s00792-006-0038-x
DO - 10.1007/s00792-006-0038-x
M3 - Article
C2 - 17082970
AN - SCOPUS:33847255445
VL - 11
SP - 277
EP - 282
JO - Extremophiles : life under extreme conditions
JF - Extremophiles : life under extreme conditions
SN - 1431-0651
IS - 2
ER -