1H, 15N and 13C Resonance Assignments for the C-terminal Protein Interaction
Region of the 32 kDa Subunit of Human Replication Protein A

Involved in interactions with DNA repair and DNA recombination proteins

1H, 15N and 13C resonance assignments for the C-terminal protein interaction region of the 32 kDa subunit of human replication protein A.

Replication protein A (RP-A) is a complex of three polypeptides of molecular
mass 70, 32, and 14 kDa, which is absolutely required for simian virus 40 DNA
replication in vitro. We have isolated a cDNA coding for the 32-kDa subunit of
RP-A. An oligonucleotide probe was constructed based upon a tryptic peptide
sequence derived from whole RP-A, and clones were isolated from a lambda gt11
library containing HeLa cDNA inserts. The amino acid sequence predicted from
the cDNA contains the peptide sequence obtained from whole RP-A along with two
sequences obtained from tryptic peptides derived from sodium dodecyl
sulfate-polyacrylamide gel-purified 32-kDa subunit. The coding sequence
predicts a protein of 29,228 daltons, in good agreement with the
electrophoretically determined molecular mass of the 32-kDa subunit. No
significant homology was found with any of the sequences in the GenBank data
base. The protein predicted from the cDNA has an N-terminal region rich in
glycine and serine along with two acidic and two basic segments. Monoclonal
antibodies have been raised against the 70- and 32-kDa subunits of RP-A. The
cloned cDNA has been overexpressed in bacteria using an inducible T7 expression
system. The protein made in bacteria is recognized by a monoclonal antibody
that is specific for the 32-kDa subunit of RP-A. This monoclonal antibody
against the 32-kDa subunit inhibits DNA replication in vitro.

Erdile, L.F., Wold, M.S., and Kelly, T.J. "The primary structure of the 32-kDA
subunit of human replication protein A". J. Biol. Chem. (1990) 265:3177-3182.

The primary structure of the 32-kDa subunit of human replication protein A.

The first 4 residues (GSHM) do not belong to the protein.
First residue (Ser 172), last residue (Glu 270)

Solution Structure Of The C-Terminal Domain Of Human Rpa32 Complexed With Ung2(73-88)

Structural Model For The Interaction Between Rpa32 C- Terminal Domain And Sv40 T Antigen Origin Binding Domain

Full-Length Replication Protein A Subunits Rpa14 And Rpa32

Crystal Structure Of Full-Length Human Rpa1432 HETERODIMER

Crystal Complex Of Rpa32c And Smarcal1 N-terminus

replication protein A2, 32kDa [synthetic construct]

Replication protein A2, 32kDa [Homo sapiens]

replication protein A 32 kDa subunit [Pongo abelii]

replication protein A 32 kDa subunit [Macaca mulatta]

replication protein A 32 kDa subunit isoform 2 [Homo sapiens]

replication protein A 32 kDa subunit isoform 3 [Homo sapiens]

replication protein A 32 kDa subunit isoform 1 [Homo sapiens]

RecName: Full=Replication protein A 32 kDa subunit; Short=RP-A p32; AltName: Full=Replication factor A protein 2; Short=RF-A pr