RAD52-RPA Interactions (literature search)

Summary     References     Sequence     Structure

 

Summary:

RPA residues

RAD52 binding site

Specific Reference

RPA34C (last 33 aa)

RAD52 (221-280)

Park (Aug. ’96)

RPA32C (172-270)

RAD52 (257-274)

Bochkareva (Oct. ’00)

RPA32C (224-271)

RAD52 (218-303)

Borgstahl (Aug. ’02)

RPA70 (169-326)

RAD52 (218-303)

Borgstahl (Aug. ’02)

 

References:

 

A. Information on specific interaction sites

 

  1. Park et al. – Aug. 1996.

RPA34C (last 33 aa) interacts with amino acids 221-280 in RAD52.

RPA34 has higher affinity to RAD52 than RPA70 and RPA14 has none.

hRAD52 (221-280) has only 7% homology in other species. (TOP)

 

  1. Hays et al. – July 1998.

RAD52 interacts with all 3 subunits of yeast RPA.

RAD52 interaction with yeast RPA70 > yRPA32 > yRPA14.

This interaction might be between yRPA70 and DNA binding domain of RAD52.

yRPA70 interacts with RAD52 but not with RAD51, RAD55 and RAD57. (TOP)

 

  1. Bochkareva et al. – Oct. 2000. – discusses many structural aspects of RPA.

RPA32C (172-270) interacts with RAD52 (257-274).

(Same paper is detailed in XPA page). (TOP)

 

  1. Borgstahl et al. – Aug. 2002.

RAD52 (218-303) binds either RPA32C (224-271) or RPA70 (169-326). (TOP)

 

  1. Shen et al. – Oct. 2002.

Park et al. paper listed above is referred. (TOP)

 

  1. Symington et al. – Oct. 2003.

Formation of RPA-RAD52-RAD59 complex suggested. (TOP)

 

B. General interaction information

 

  1. Berg at al. – Mar. 1995.
  2. Kowalczykowski et al. – Jan. 1998.
  3. Kowalczykowski et al. – May 1998.
  4. Shinohara et al. – Mar. 1998.
  5. Shinohara et al. – Jul. 1998.
  6. Sung et al. – May 2000.
  7. Watts et al. – Oct. 2001.
  8. Symington et al. – Jun. 2002.
  9. Nicolas et al. – Jun. 2002.
  10. Kowalczykowski et al. – Aug. 2002.
  11. Haber et al. – Dec. 2003.                                                                                 (TOP)

 

C. hRAD52 Full Sequence

 

Source: AAS00097 – hRAD52 on NCBI protein sequence database [gi: 41324138].

 

  1 MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ KALRQRLGPE YISSRMAGGG

 61 QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN GKFYVGVCAF VRVQLKDGSY

121 HEDVGYGVSE GLKSKALSLE KARKEAVTDG LKRALRSFGN ALGNCILDKD YLRSLNKLPR

181 QLPLEVDLTK AKRQDLEPSV EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS

241 SRSLSSSAVE SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST

301 PVTVSEPLLE KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD PAQTSDTLAL

361 NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN WESHRKSQDM KKRKYDPS

 

D. RAD52 Structure

 

  1. 1H2I – hRAD52 N- Terminal Domain from PDB.
  2. 1KN0 – hRAD52 N-Terminal Domain from PDB.
  3. 1DPU – RPA32C + UNG2(73-88) complex. {UNG2(73-88)≡RAD52(257-274).
  4. Secondary Structure predicted by SABLE server : RAD52.

 

RAD52 interacts with RPA32C and RPA70(169-326) domains, whose tertiary structures have been determined.

Please click on the links below to view the domains:

 

1.      RPA32C – Figure obtained through VMD. (or check 1DPU in PDB)

2.      RPA70(181-432) – Figure obtained through VMD. (or check 1FGU in PDB)