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Literature summary for 2.7.7.7 extracted from

  • Bauer, R.J.; Wolff, I.D.; Zuo, X.; Lin, H.K.; Trakselis, M.A.
    Assembly and distributive action of an archaeal DNA polymerase holoenzyme (2013), J. Mol. Biol., 425, 4820-4836.
    View publication on PubMed
Search for more literature for 2.7.7.7

Cloned(Commentary)

Cloned (Comment) Organism
-
 Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-
Saccharolobus solfataricus P2
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn ATP binding to replication factor C is sufficient for loading the heterotrimeric PCNA123 [proliferating cell nuclear antigen (PCNA)] clamp onto DNA that includes a rate-limiting conformational rearrangement of the complex. ATP hydrolysis is required for favorable recruitment and interactions with the replication polymerase (PolB1) that most likely include clamp closing and dissociation of replication factor C. Surprisingly, the assembled holoenzyme complex synthesizes DNA distributively and with low processivity, unlike most other well-characterized DNA polymerase holoenzyme complexes. PolB1 repeatedly disengages from the DNA template, leaving PCNA123 behind. Interactions with a C-terminal PCNA-interacting peptide (PIP) motif on PolB1 specifically with PCNA2 are required for holoenzyme formation and continuous re-recruitment during synthesis Saccharolobus solfataricus diphosphate + DNAn+1
-
 ?
deoxynucleoside triphosphate + DNAn ATP binding to replication factor C is sufficient for loading the heterotrimeric PCNA123 [proliferating cell nuclear antigen (PCNA)] clamp onto DNA that includes a rate-limiting conformational rearrangement of the complex. ATP hydrolysis is required for favorable recruitment and interactions with the replication polymerase (PolB1) that most likely include clamp closing and dissociation of replication factor C. Surprisingly, the assembled holoenzyme complex synthesizes DNA distributively and with low processivity, unlike most other well-characterized DNA polymerase holoenzyme complexes. PolB1 repeatedly disengages from the DNA template, leaving PCNA123 behind. Interactions with a C-terminal PCNA-interacting peptide (PIP) motif on PolB1 specifically with PCNA2 are required for holoenzyme formation and continuous re-recruitment during synthesis Saccharolobus solfataricus P2 diphosphate + DNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
POlB1
-
 Saccharolobus solfataricus