GroEL - Protein Interaction Database

Proteins that interact with GroEL and factors that affect their release



This table is simply designed to show the diverse nature of GroEL substrates. It is not intended to be an all inclusive bibliographic reference. Citations given are generally for the earliest documentation for that substrate.

If you know of substrates not listed below, please forward that information to Jeff Seale

The first 31 entries in this database were compiled by Boris Gorovits

N/A in the Release requirements means that the cited reference may not have determined this information



Protein

Release requirements

Reference
alcohol oxidase MgATP
(1)
alpha-glucosidase MgATP
(2)
alpha-lactalbumin N/A
(3)
aspartate aminotransferase MgATP + GroES or MgATP
(4)
barnase MgATP or none
(5)
beta-lactamase precursor MgATP + GroES
(6)
chloramphenicol
acetyltransferase		 GroE system not required
(7)
chloroplast precursor protein GroES + MgATP; casein + MgATP
(8)
citrate synthase GroES + MgATP
(9)
CRAG ATP
(10)
cyclophilin GroES + MgADP
(11)
Cu,Zn superoxide dismutase N/A
(12)
dihydrofolate reductase MgATP required; GroES helps
(13)
dodecameric glutamine synthase MgATP; or MgADP + GroES
(14)
E2 inner core bovine
mitochondrial branched chain
a-keto acid dehydrogenase		 GroES + MgATP
(15)
F(ab) fragments GroES + MgATP
(16)
glucose-6-phosphate dehydrogenase none, or MgATP
(17)
granulocyte RNase MgATP
(18)
lactate dehydrogenase MgATP or MgAMP-PNP
(19)
luciferase this study in vivo
(20)
malate dehydrogenase MgATP; K+ is not obligatory
(21)
non-glycosylated invertase MgATP; GroES helps; glyco form
does not interact
(22)
ornithine transcarbamylase GroES + MgATP
ATP analogues with GroES do not work
(23)
phytochrome photoreceptor MgATP
(24)
RNA polymerase GroES + MgATP (?)
(25)
RUBISCO GroES + MgATP
(26)
RNA polymerase, sigma subunit N/A
(27)
ssDNA binding protein N/A
(28)
tryptophanase ATP, ADP, AMP-PNP
(29)
tubulins GroES + MgATP
(30)
yeast enolase MgATP; or MgADP + GroES
(31)
Taka-amylase A GroES + ATP or ADP
(32)
E. coli B-galactosidase GroEL reduces aggregation, GroEL+ ATP or AMP-PNP
leads to aggregation
(33)
rhodanese GroES + MgATP & K+
(34)
carbonic anhydrase II
(35)
prion protein PrPc not determined
(36)
NiFe hydrogenase 3 precursor not determined
(37)
glycerol dehydrogenase ATP increases kinetics; GroES not required
(38)
trichosanthin Mg, ATP
(39)
staphylococcal nuclease ATP accelerates refolding; ATP+GroES maximal refolding
(40)



This information is accurate to the best of my knowledge. However, you should check the references cited for a more complete understanding of these substrates and their interactions with GroEL.



References


  1. Evers et al (1993) FEBS Letts 321: 32-36.
  2. Holl-Neugebert et al (1991) Biochemistry 30: 11609-11614.
  3. Hayer-Hartl et al (1994) EMBO J 13: 3192-3202.
  4. Mattingly et al (1995) J. Biol. Chem. 270: 1138-1148.
  5. Gray et al (1993) J. Mol. Biol. 232: 1197-1207.
  6. Laminet et al (1990) EMBO J. 9: 2315-2319.
  7. Kim & Kang (1991) Biochem. Intl 25: 381-386.
  8. Dessauer et al (1994) J. Biol. Chem. 269: 19766-19776.
  9. Buchner et al (1991) Biochemistry 30: 1586-1591.
  10. Sherman & Goldberg (1991) J. Bacteriol. 173: 7249-7256.
  11. Zahn et al (1994) Nature 368: 261-265.
  12. Battistoni et al (1993) FEBS Letts 322: 6-9.
  13. Viitanen et al (1991) Biochemistry 30: 9716-9723.
  14. Fisher (1992) Biochemistry 31: 3955-3963.
  15. Wynn et al (1994) Biochemistry 33: 8962-8968.
  16. Schmidt & Buchner (1992) J. Biol. Chem. 267: 16829-16833.
  17. Hansen & Gafni (1993) J. Biol. Chem. 268: 21632-21636.
  18. Rosenberg et al (1993) J. Biol. Chem. 268: 4499-4503.
  19. Badcoe et al (1991) Biochemistry 30: 9195-9200.
  20. Escher et al (1993) Mol. Gen. Genet. 238: 65-73.
  21. Miller et al (1993) Biochem. J. 291: 139-144.
  22. Kern et al (1992) FEBS Letts. 305: 203-205.
  23. Zheng et al (1993) J. Biol. Chem. 268: 7489-7493.
  24. Grimm et al (1993) J. Biol. Chem. 268: 5220-5226.
  25. Ziemienowicz et al (1993) J. Biol. Chem. 268: 25425-25431.
  26. Viitanen et al (1990) Biochemistry 29: 5665-5671.
  27. Brown et al (1992) Mol. Microbiol. 6: 1133-1139.
  28. Laine et al (1992) J. Bacteriol. 174: 3204-3211.
  29. Mizobata et al (1992) J. Biol. Chem. 267: 17773-17779.
  30. Phadtare et al (1994) Biochem. Biophys. Acta 1208: 189-192.
  31. Kubo et al (1993) J. Biol. Chem. 268: 19346-19351.
  32. Kawata et al (1994) FEBS Letts 345: 229-232.
  33. Ayling & Baneyx (1996) Prot. Sci. 5: 478-487.
  34. Mendoza et al (1991) J. Biol. Chem. 266: 13044-13049.
  35. Persson et al (1995) Biochem. Biophys. Acta 1247: 195-200.
  36. Edenhofer et al (1996) J. Virology. 70: 4724-4728.
  37. Rodrigue et al (1996) J. Bacteriol. 178: 4453-4460.
  38. Krauss & Gore (1996) Eur. J. Biochem. 241: 538-545.
  39. Lau et al (1998) Biochem. Biophys. Res. Comm. 245: 149-154.
  40. Tsurupa et al (1998) J. Mol. Biol. 277: 733-745.





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Last Updated May 26, 1998