High Confidence Fission Yeast SUMO Conjugates Identified by Tandem Denaturing Affinity Purification

Nie, Minghua; Vashisht, Ajay A.; Wohlschlegel, James A.; Boddy, Michael N.

doi:10.1038/srep14389

Cited by 13 publications

(13 citation statements)

References 59 publications

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“…These data indicate that all SUMOylation components are indispensable for SUMOylation. The pleiotrophic phenotypes of the deletion mutants may be a result of the dysfunction of SUMOylation, because SUMOylated proteins play roles in chromatin organization, transcriptional regulation, RNA biosynthesis and ribosome biogenesis (Nie et al ., ).…”

Section: Discussionmentioning

confidence: 97%

SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae

Lim

Kim

Lee

2018

Molecular Plant Pathology

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Amongst the various post-translational modifications (PTMs), SUMOylation is a conserved process of attachment of a small ubiquitin-related modifier (SUMO) to a protein substrate in eukaryotes. This process regulates many important biological mechanisms, including transcriptional regulation, protein stabilization, cell cycle, DNA repair and pathogenesis. However, the functional role of SUMOylation is not well understood in plant-pathogenic fungi, including the model fungal pathogen Magnaporthe oryzae. In this study, we elucidated the roles of four SUMOylation-associated genes that encode one SUMO protein (MoSMT3), two E1 enzymes (MoAOS1 and MoUBA2) and one E2 enzyme (MoUBC9) in fungal development and pathogenicity. Western blot assays showed that SUMO modification was abolished in all deletion mutants. MoAOS1 and MoUBA2 were mainly localized in the nucleus, whereas MoSMT3 and MoUBC9 were localized in both the nucleus and cytoplasm. However, the four SUMOylation-associated proteins were predominantly localized in the nucleus under oxidative stress conditions. Deletion mutants for each of the four genes were viable, but showed significant defects in mycelial growth, conidiation, septum formation, conidial germination, appressorium formation and pathogenicity. Several proteins responsible for conidiation were predicted to be SUMOylated, suggesting that conidiation is controlled at the post-translational level by SUMOylation. In addition to infection-related development, SUMOylation also played important roles in resistance to nutrient starvation, DNA damage and oxidative stresses. Therefore, SUMOylation is required for infection-related fungal development, stress responses and pathogenicity in M. oryzae. This study provides new insights into the role of SUMOylation in the molecular mechanisms of pathogenesis of the rice blast fungus and other plant pathogens.

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Section: Discussionmentioning

confidence: 97%

SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae

Lim

Kim

Lee

2018

Molecular Plant Pathology

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“…Identification of the effect(s) of sumoylation on individual proteins has, in many cases proved problematic. For example, there are a number of well-studied cases where several members of multiprotein complexes are all sumoylated ( Jentsch and Psakhye, 2013 ; Nie et al, 2015 ). In such cases, inability to sumoylate a single member of the complex has little affect because sumoylation of other components of the complex is sufficient for function.…”

Section: Discussionmentioning

confidence: 99%

Sumoylation of eIF4A2 affects stress granule formation

Jongjitwimol

Baldock

Morley

et al. 2016

Journal of Cell Science

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Regulation of protein synthesis is crucial for cells to maintain viability and to prevent unscheduled proliferation that could lead to tumorigenesis. Exposure to stress results in stalling of translation, with many translation initiation factors, ribosomal subunits and mRNAs being sequestered into stress granules or P bodies. This allows the re-programming of the translation machinery. Many aspects of translation are regulated by post-translational modification. Several proteomic screens have identified translation initiation factors as targets for sumoylation, although in many cases the role of this modification has not been determined. We show here that eIF4A2 is modified by SUMO, with sumoylation occurring on a single residue (K226). We demonstrate that sumoylation of eIF4A2 is modestly increased in response to arsenite and ionising radiation, but decreases in response to heat shock or hippuristanol. In arsenite-treated cells, but not in hippuristanol-treated cells, eIF4A2 is recruited to stress granules, suggesting sumoylation of eIF4A2 correlates with its recruitment to stress granules. Furthermore, we demonstrate that the inability to sumoylate eIF4A2 results in impaired stress granule formation, indicating a new role for sumoylation in the stress response.

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“…There is a precedent for such STUbL recruitment, in the recognition and ubiquitylation of unmodified budding yeast Matα2 by Slx5-Slx8 [ 60 , 61 ]. However, Rad60 is modified by SUMO [ 62 ], and so a similar modification of Esc2 could enhance STUbL recruitment at replication forks.…”

Section: Sumo Mimicry Integrates Sumo and Ubiquitin Signaling In Dmentioning

confidence: 99%

Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability

Nie

Boddy

2016

Biomolecules

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Covalent attachment of ubiquitin (Ub) or SUMO to DNA repair proteins plays critical roles in maintaining genome stability. These structurally related polypeptides can be viewed as distinct road signs, with each being read by specific protein interaction motifs. Therefore, via their interactions with selective readers in the proteome, ubiquitin and SUMO can elicit distinct cellular responses, such as directing DNA lesions into different repair pathways. On the other hand, through the action of the SUMO-targeted ubiquitin ligase (STUbL) family proteins, ubiquitin and SUMO can cooperate in the form of a hybrid signal. These mixed SUMO-ubiquitin chains recruit “effector” proteins such as the AAA+ ATPase Cdc48/p97-Ufd1-Npl4 complex that contain both ubiquitin and SUMO interaction motifs. This review will summarize recent key findings on collaborative and distinct roles that ubiquitin and SUMO play in orchestrating DNA damage responses.

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High Confidence Fission Yeast SUMO Conjugates Identified by Tandem Denaturing Affinity Purification

Cited by 13 publications

References 59 publications

SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae

SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae

Sumoylation of eIF4A2 affects stress granule formation

Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability

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