Crossref journal-article
Wiley
FEBS Letters (311)
Abstract

Proteasomes are the major protein‐degrading complexes in the cytosol and regulate many cellular processes. To examine the functional importance of the MC14/MECL‐1 proteasome active site subunits, cell lines expressing a catalytically inactive form of MECL‐1 were established. Whereas mutant MECL‐1 was readily incorporated into cytosolic proteasomes, replacing the constitutive MC14 subunit, removal of the prosequence was incomplete indicating that its processing required autocatalytic cleavage. Functional analyses showed that the absence of the MC14/MECL‐1 active sites abrogated proteasomal trypsin‐like activity, but did not affect other catalytic activities. Our data demonstrate a conservation of cleavage specificity between mammalian and yeast proteasomes.

Bibliography

Salzmann, U., Kral, S., Braun, B., Standera, S., Schmidt, M., Kloetzel, P.-M., & Sijts, A. (1999). Mutational analysis of subunit iβ2 (MECL‐1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes. FEBS Letters, 454(1–2), 11–15. Portico.

Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 8:18 a.m.)
Deposited 1 year, 11 months ago (Sept. 16, 2023, 8:39 a.m.)
Indexed 4 months, 4 weeks ago (March 31, 2025, 4:42 a.m.)
Issued 26 years, 1 month ago (July 2, 1999)
Published 26 years, 1 month ago (July 2, 1999)
Published Online 26 years, 1 month ago (July 6, 1999)
Published Print 26 years, 1 month ago (July 2, 1999)
Funders 0

None

@article{Salzmann_1999, title={Mutational analysis of subunit iβ2 (MECL‐1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes}, volume={454}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(99)00768-1}, DOI={10.1016/s0014-5793(99)00768-1}, number={1–2}, journal={FEBS Letters}, publisher={Wiley}, author={Salzmann, Ulrike and Kral, Sylvie and Braun, Beate and Standera, Sybille and Schmidt, Marion and Kloetzel, Peter-M and Sijts, Alice}, year={1999}, month=jul, pages={11–15} }