The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function
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The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function. / Ruidiaz, Sarah F.; Dreier, Jesper E.; Hartmann-Petersen, Rasmus; Kragelund, Birthe B.
I: Protein Science, Bind 30, Nr. 10, 2021, s. 2069-2082.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function
AU - Ruidiaz, Sarah F.
AU - Dreier, Jesper E.
AU - Hartmann-Petersen, Rasmus
AU - Kragelund, Birthe B.
PY - 2021
Y1 - 2021
N2 - Intrinsically disordered proteins (IDPs) regularly constitute components of larger protein assemblies contributing to architectural stability. Two small, highly acidic IDPs have been linked to the so-called PCI complexes carrying PCI-domain subunits, including the proteasome lid and the COP9 signalosome. These two IDPs, DSS1 and CSNAP, have been proposed to have similar structural propensities and functions, but they display differences in their interactions and interactome sizes. Here we characterized the structural properties of human DSS1 and CSNAP at the residue level using NMR spectroscopy and probed their propensities to bind ubiquitin. We find that distinct structural features present in DSS1 are completely absent in CSNAP, and vice versa, with lack of relevant ubiquitin binding to CSNAP, suggesting the two proteins to have diverged in both structure and function. Our work additionally highlights that different local features of seemingly similar IDPs, even subtle sequence variance, may endow them with different functional traits. Such traits may underlie their potential to engage in multiple interactions thereby impacting their interactome sizes.
AB - Intrinsically disordered proteins (IDPs) regularly constitute components of larger protein assemblies contributing to architectural stability. Two small, highly acidic IDPs have been linked to the so-called PCI complexes carrying PCI-domain subunits, including the proteasome lid and the COP9 signalosome. These two IDPs, DSS1 and CSNAP, have been proposed to have similar structural propensities and functions, but they display differences in their interactions and interactome sizes. Here we characterized the structural properties of human DSS1 and CSNAP at the residue level using NMR spectroscopy and probed their propensities to bind ubiquitin. We find that distinct structural features present in DSS1 are completely absent in CSNAP, and vice versa, with lack of relevant ubiquitin binding to CSNAP, suggesting the two proteins to have diverged in both structure and function. Our work additionally highlights that different local features of seemingly similar IDPs, even subtle sequence variance, may endow them with different functional traits. Such traits may underlie their potential to engage in multiple interactions thereby impacting their interactome sizes.
KW - IDP
KW - interactomes
KW - NMR
KW - proteasome
KW - signalosome
KW - ubiquitin
KW - CATION-PI INTERACTIONS
KW - MESSENGER-RNA EXPORT
KW - 26S PROTEASOME
KW - UNSTRUCTURED PROTEINS
KW - REGULATORY PARTICLE
KW - INTRINSIC DISORDER
KW - 2-DIMENSIONAL NMR
KW - CANDIDATE GENE
KW - SEM1
KW - COMPLEXES
U2 - 10.1002/pro.4159
DO - 10.1002/pro.4159
M3 - Journal article
C2 - 34272906
VL - 30
SP - 2069
EP - 2082
JO - Protein Science
JF - Protein Science
SN - 0961-8368
IS - 10
ER -
ID: 275937309