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Study results show that although human DNA primase C-terminal domain (p58C) can be stabilized in different conformations in the crystalline state, in solution there is effectively no difference in the structure and functional properties of p58C constructs of different lengths.
Data suggest that PRIM1-p58,C-terminal domain stays bound to initiating NTP and 3prime-overhang DNA during whole cycle of RNA primer synthesis; meanwhile, PRIM1-p49 slides along DNA template toward 5prime-end with PRIM1-p58,N-terminal domain attached.
Data indicate that the conformational changes in primase are necessary to accomplish the initiation and then elongation of RNA synthesis.
the N-terminal domain of the large subunit of primase (p58N) directly interacts with the C-terminal domain of the catalytic subunit of polalpha (p180C)
PRIM2 gene is not imprinted in the placenta.
The fragment that forms a beta-sheet in the reported structure p58C/3L9Q of the same human primase domain is folded in three alpha-helices in our p58C/3Q36 structure, similarly to yeast primase.
p58C(C-terminal regulatory domain of the large subunit) structure reveals a novel arrangement of an evolutionarily conserved 4Fe-4S cluster buried deeply within the protein core and is not similar to any known protein structure.
analysis of the iron-sulfur cluster in the C-terminal domain of the p58 subunit of human DNA primase
The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components. Primase, which is a heterodimer of a small subunit and a large subunit, synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. The protein encoded by this gene is the large, 58 kDa primase subunit.
DNA primase, p58 subunit
, DNA primase 58 kDa subunit
, DNA primase large subunit
, DNA polymerase alpha subunit III (primase)
, DNA primase subunit p58
, primase polypeptide 2A, 58kDa
, primase, polypeptide 2A, 58kDa
, DNA primase polypeptide 2