Letter :Slippery substrates impair ATP-dependent protease function by slowing unfolding

Journal of Biological Chemistry

Volumn 289, Issue 6, 2014, Pages 3826-

  Coffino, Philip ^a   Too, Priscilla Hiu Mei ^a,b   Erales, Jenny ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Campus de Luminy ^*  (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN;

CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; HUMAN; NOTE;

ADENOSINE TRIPHOSPHATASES; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; MOLECULAR CHAPERONES;

EID: 84893661697     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.L113.532622     Document Type: Letter

References (5)

1. Too, P. H., Erales, J., Simen, J. D., Marjanovic, A., and Coffino, P. (2013) Slippery substrates impair function of a bacterial protease ATPase by unbalancing translocation versus exit. J. Biol. Chem. 288, 13243-13257
2. Kraut, D. A. (2013) Slippery substrates impair ATP-dependent protease function by slowing unfolding. J. Biol. Chem. 288, 34729-34735
3. Hoyt, M. A., Zich, J., Takeuchi, J., Zhang, M., Govaerts, C., and Coffino, P. (2006) Glycine-Alanine repeats impair proper substrate unfolding by the proteasome. EMBO J. 25, 1720-1729
4. Zhang, M., and Coffino, P. (2004) Repeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processing. J. Biol. Chem. 279, 8635-8641
5. Kraut, D. A., Israeli, E., Schrader, E. K., Patil, A., Nakai, K., Nanavati, D., Inobe, T., and Matouschek, A. (2012) Sequence-And species-dependence of proteasomal processivity. ACS Chem. Biol. 7, 1444-1453