scholarly journals Identification of proximal SUMO-dependent interactors using SUMO-ID

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Orhi Barroso-Gomila ◽  
Fredrik Trulsson ◽  
Veronica Muratore ◽  
Iñigo Canosa ◽  
Laura Merino-Cacho ◽  
...  
Keyword(s):  
Dna Damage ◽  
Stress Response ◽  
Posttranslational Modifications ◽  
Protein Fragment ◽  
Sumo Modification ◽  
Protein Fragment Complementation ◽  
Fragment Complementation

AbstractThe fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We develop an optimized split-TurboID version and show SUMO interaction-dependent labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors of PML are involved in transcription, DNA damage, stress response and SUMO modification and are highly enriched in SUMO Interacting Motifs, but may only represent a subset of the total PML proximal proteome. Likewise, SUMO-ID also allow us to identify interactors of SUMOylated SALL1, a less characterized SUMO substrate. Furthermore, using TP53 as a substrate, we identify SUMO1, SUMO2 and Ubiquitin preferential interactors. Thus, SUMO-ID is a powerful tool that allows to study the consequences of SUMO-dependent interactions, and may further unravel the complexity of the ubiquitin code.

scholarly journals Identification of proximal SUMO-dependent interactors using SUMO-ID

2020 ◽  
Author(s):  
Orhi Barroso-Gomila ◽  
Fredrik Trulsson ◽  
Veronica Muratore ◽  
Iñigo Canosa ◽  
Ana Rosa Cortazar ◽  
...  
Keyword(s):  
Dna Damage ◽  
Stress Response ◽  
Posttranslational Modifications ◽  
Protein Fragment ◽  
Sumo Modification ◽  
Protein Fragment Complementation ◽  
Fragment Complementation

ABSTRACTThe fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We developed an optimized split-TurboID version and show SUMO interaction-dependent labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors of PML are involved in transcription, DNA damage, stress response and SUMO modification and are highly enriched in SUMO Interacting Motifs, but may only represent a subset of the total PML proximal proteome. Likewise, SUMO-ID also allowed us to identify novel interactors of SUMOylated SALL1, a less characterized SUMO substrate. Thus, SUMO-ID is a powerful tool that allows to study the consequences of SUMO-dependent interactions, and may further unravel the complexity of the ubiquitin code.

Universal strategies in research and drug discovery based on protein-fragment complementation assays

2007 ◽  
Vol 6 (7) ◽  
pp. 569-582 ◽  
Author(s):  
Stephen W. Michnick ◽  
Po Hien Ear ◽  
Emily N. Manderson ◽  
Ingrid Remy ◽  
Eduard Stefan
Keyword(s):  
Drug Discovery ◽  
Protein Fragment ◽  
Protein Fragment Complementation ◽  
Fragment Complementation

scholarly journals Sensitive detection of protein ubiquitylation using a protein fragment complementation assay

2020 ◽  
Vol 133 (12) ◽  
pp. jcs240093 ◽  
Author(s):  
Marie Le Boulch ◽  
Audrey Brossard ◽  
Gaëlle Le Dez ◽  
Sébastien Léon ◽  
Gwenaël Rabut
Keyword(s):  
Sensitive Detection ◽  
Protein Fragment ◽  
Complementation Assay ◽  
Protein Fragment Complementation ◽  
Fragment Complementation ◽  
Protein Fragment Complementation Assay

Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation

2014 ◽  
Vol 50 (15) ◽  
pp. 1830-1832 ◽  
Author(s):  
Xiongfeng Dai ◽  
Manlu Zhu ◽  
Yi-Ping Wang
Keyword(s):  
Catalytic Activity ◽  
Circular Permutation ◽  
Protein Fragment ◽  
Epsp Synthase ◽  
E Coli ◽  
Protein Fragment Complementation ◽  
Fragment Complementation ◽  
Inhibitor Resistance

Circular permutation can increase an enzyme's inhibitor resistance and is a good indicator for establishing protein fragment complementation.

scholarly journals Antibody library selection by the β-lactamase protein fragment complementation assay

2008 ◽  
Vol 22 (3) ◽  
pp. 149-158 ◽  
Author(s):  
Paola Secco ◽  
Elena D'Agostini ◽  
Roberto Marzari ◽  
Marta Licciulli ◽  
Roberto Di Niro ◽  
...  
Keyword(s):  
Antibody Library ◽  
Protein Fragment ◽  
Complementation Assay ◽  
Protein Fragment Complementation ◽  
Fragment Complementation ◽  
Protein Fragment Complementation Assay ◽  
Library Selection
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