Structure, Volume 28

Supplemental Information

Characterization of a C-Terminal

SUMO-Interacting Motif Present

in Select PIAS-Family Proteins

Mathieu Lussier-Price, Xavier H. Mascle, Laurent Cappadocia, Rui Kamada, KazuyasuSakaguchi, Haytham M. Wahba, and James G. Omichinski

Characterization of C-terminal SIM in PIAS-family proteins

1

Supplemental Information Functional and structural characterization of a novel

C-terminal SUMO-interacting motif present in PIAS-

family proteins.

Mathieu Lussier-Price1, Xavier H. Mascle1, Laurent Cappadocia1, 4, Kazuyasu

Sakaguchi3, Haytham M. Wahba1,3 and James G. Omichinski1,5 *

1Département de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC

H3C 3J7, Canada, 2Department of Biochemistry, Beni-Suef University, Beni-Suef 62521, Egypt

and 3 Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810,

Japan.

4 Current Address : Département de Chimie, Université de Québec à Montréal, Montréal, QC, H2X

2J6 Canada

5 Lead Contact

*Correspondence:

James G. Omichinski, Département de Biochimie et Médicine Moléculaire, Université de

Montréal C.P. 6128 Succursale Centre-Ville, Montréal, QC H3C 3J7 Canada. Email:

jg.omichinski@umontreal.ca

Running Title: Characterization of C-terminal SIM in PIAS-family proteins

Characterization of C-terminal SIM in PIAS-family proteins

2

Inventory of Supplemental Information:

Figure S1 related to Figure 3: Structure of the ΔN-SUMO1 in complex with the mPIAS-SIM2

in the un-phosphorylated and phosphorylated form.

Figure S2 related to Figure 5: Structure of the K37Ac variant of ΔN-SUMO1 in complex with

the mPIAS-SIM2 in the un-phosphorylated and phosphorylated form.

Characterization of C-terminal SIM in PIAS-family proteins

3

Figure S1 related to Figure 3. Structure of the ΔN-SUMO1 in complex with the mPIAS-SIM2 in the un-phosphorylated and phosphorylated form. Electron density map corresponding to residues of the core and C-terminal region of the SIM2 of PIAS in (A) the ΔN-SUMO1:mPIAS-SIM2 complex and (B) the ΔN-SUMO1:mPIAS-SIM2-PO4 complex. The peptides are in stick representation with carbon atoms colored in blue (mPIAS-SIM2) and yellow (mPIAS-SIM2-PO4). The 2FoFc electron density map, contoured at 1.3σ, is represented by a gray mesh.

Characterization of C-terminal SIM in PIAS-family proteins

4

Figure S2 related to Figure 5. Structure of the K37Ac variant of ΔN-SUMO1 in complex with the mPIAS-SIM2 in the un-phosphorylated and phosphorylated form. Top: Structure of the ΔN-SUMO1-K37Ac:mPIAS-SIM2 (A) and ΔN-SUMO1-K37Ac:mPIAS-SIM2-PO4 (B) complex showing an overview of the interactions between ΔN-SUMO1-K37Ac and residues 617-621 of the SIM peptides. The proteins are in cartoon representation with ΔN-SUMO1 carbon atoms in gray, mPIAS-SIM2 peptide carbon atoms in blue and the mPIAS-SIM2-PO4 peptide carbon atoms in yellow. The residues of interest are in stick representation. Bottom: Electron density map corresponding to residues of the core and C-terminal region of the SIM2 of PIAS in (A) the ΔN-SUMO1-K37Ac:mPIAS-SIM2 complex and (B) the ΔN-SUMO1K37Ac:mPIAS-SIM2-PO4 complex. The 2FoFc electron density map, contoured at 1.3σ, is represented by a gray mesh.