B.H.Ha
et al.
(2016).
The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity.
Biochem Biophys Res Commun,
476,
450-456.
PubMed id: 27240952
DOI: 10.1016/j.bbrc.2016.05.143
The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity.
B.H.Ha,
K.H.Kim,
H.M.Yoo,
W.Lee,
E.EunKyeong Kim.
ABSTRACT
Ubiquitin-fold modifier 1 (Ufm1) specific protease (UfSP) is a novel cysteine
protease that activates Ufm1 from its precursor by processing the C-terminus to
expose the conserved Gly necessary for substrate conjugation and de-conjugates
Ufm1 from the substrate. There are two forms: UfSP1 and UfSP2, the later with an
additional domain at the N-terminus. Ufm1 and both the conjugating and
deconjugating enzymes are highly conserved. However, in Caenorhabditis elegans
there is one UfSP which has extra 136 residues at the N terminus compared to
UfSP2. The crystal structure of cUfSP reveals that these additional residues
display a MPN fold while the rest of the structure mimics that of UfSP2. The MPN
domain does not have the metalloprotease activity found in some MPN-domain
containing protein, rather it is required for the recognition and deufmylation
of the substrate of cUfSP, UfBP1. In addition, the MPN domain is also required
for localization to the endoplasmic reticulum.
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