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Cathepsin S, but not cathepsin L, participates in the MHC class II-associated invariant chain processing in large yellow croaker (Larimichthys crocea).

Li Q1, Ao J2, Mu Y3, Yang Z3, Li T3, Zhang X3, Chen X3.
Fish & shellfish immunology.Fish Shellfish Immunol.2015 Dec;47(2):743-50. doi: 10.1016/j.fsi.2015.10.009. Epub 2015 Oct 22.
Two cysteine proteases, cathepsin S (CatS) and cathepsin L (CatL), have been identified as the key enzymes involved in the processing of invariant chain (Ii chain) in mammals. However, little is known about the roles of fish cathepsins in the Ii chain processing. In this study, large yellow croaker
PMID 26475363

Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly.

Li X1, Li Y1, Arendt CS2, Hochstrasser M3.
The Journal of biological chemistry.J Biol Chem.2015 Dec 1. pii: jbc.M115.677047. [Epub ahead of print]
Eukaryotic 20S proteasome assembly remains poorly understood. The subunits stack into four heteroheptameric rings; three inner-ring subunits (β1, β2, and β5) bear the protease catalytic residues and are synthesized with N-terminal propeptides. These propeptides are removed autocatalytically late
PMID 26627836

Maturation of Fibrinolytic Bacillopeptidase F Involves both Hetero- and Autocatalytic Processes.

Meng D1, Dai M2, Xu BL2, Zhao ZS2, Liang X2, Wang M2, Tang XF3, Tang B4.
Applied and environmental microbiology.Appl Environ Microbiol.2015 Oct 23;82(1):318-27. doi: 10.1128/AEM.02673-15.
Bacillopeptidase F (Bpr) is a fibrinolytic serine protease produced by Bacillus subtilis. Its precursor is composed of a signal peptide, an N-terminal propeptide, a catalytic domain, and a long C-terminal extension (CTE). Several active forms of Bpr have been previously reported, but little is known
PMID 26497454