Structural highlights
Function
[PRIS_SULSO] Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.[1] [PRIL_SULSO] Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.[2]
References
- ↑ Lao-Sirieix SH, Bell SD. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities. J Mol Biol. 2004 Dec 10;344(5):1251-63. PMID:15561142 doi:http://dx.doi.org/10.1016/j.jmb.2004.10.018
- ↑ Lao-Sirieix SH, Bell SD. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities. J Mol Biol. 2004 Dec 10;344(5):1251-63. PMID:15561142 doi:http://dx.doi.org/10.1016/j.jmb.2004.10.018
