DNAPK-RPA Interactions (literature search)
Summary References Sequence Structure
|
RPA residues |
DNA-PK binding site |
Specific Reference |
|
RPA32 (Thr-21 & Ser-33 are phosphorylated) |
DNA-PK§ |
Hurwitz (May 97) |
|
More RPA32 phosphorylation sites (T21, S23, S29, S33, S11/12/13, S8, S4) |
DNA-PK§ |
Dixon (Sep. 97) |
|
RPA70 |
DNA-PKcs§ |
Pommier
(Mar. 99) |
§ - Exact domains of interaction are yet to be determined.
A. Information on specific
interaction sites
DNA-PK tends to phosphorylate a Ser/Thr residue that is followed by a Glutamine residue (S/T-Q). (TOP)
All phosphorylation by DNA-PK in vitro occurs on RPA32 Nterminal (1-33 aa).
RPA32 Serines 33, 52, 72, 174 fit the consensus sequence (S/T-Q) for DNA-PK.
(TOP)
DNA-PK phosphorylates RPA32 at Thr-21 and Ser-33.
Other Serines in RPA32 (1-37) are not phosphorylated by DNA-PK. (TOP)
UV radiation causes hyperphosphorylation of RPA32N at following sites:
Thr-21, Ser-23, Ser-29, Ser-33, one of the three Ser-11/12/13.
Other probable sites are Ser-8 and Ser-4. (TOP)
DNA-PK consists of a catalytic subunit (DNA-PKcs) and the Ku autoantigen.
DNA-PKcs can form a multiprotein complex with RPA in untreated cells.
DNA-PKcs complexes with Ku (not RPA) in camptothecin treated cells.
RPA70 and DNAPKcs domains are essential for RPA:DNA-PK complex. (TOP)
B. General interaction information
Source: P78527 DNA-PKcs on NCBI protein sequence database [gi: 38258929].
The
tertiary structure of DNA-PK is yet to be determined. Interested people can
obtain the secondary structure using SABLE
(secondary structure prediction server). The protein is too big to be shown
here.
The
tertiary structure of the RPA32 N-terminal domain is also yet to be determined. (TOP)