High Mobility Group Nucleosomal Binding Domain 2 (HMGN2) SUMOylation by the SUMO E3 Ligase PIAS1 Decreases the Binding Affinity to Nucleosome Core Particles

Wu, Jie; Kim, Sol; Kwak, Man Sup; Jeong, Jang Bin; Min, Hyun Jin; Yoon, Ho Geun; Ahn, Jin-Hyun; Shin, Jeon Soo

doi:10.1074/jbc.m114.555425

Cited by 15 publications

(19 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HMGN2 has been well studied for its regulatory roles in general chromatin functions by altering nucleosome structures 36 37 . Although, the deletion of HMGN2 gene alone might not induce dramatic changes of genome wide transcription profile 38 , the encoded protein was reported to serve as a transcriptional modulator for a certain subset of genes involved in Wnt/β catenin signaling and Jak2/Stat5a pathways 39 40 .…”

Section: Resultsmentioning

confidence: 99%

The modulation of MiR-155 and MiR-23a manipulates Klebsiella pneumoniae Adhesion on Human pulmonary Epithelial cells via Integrin α5β1 Signaling

Teng

Miao

Shen

et al. 2016

Sci Rep

View full text Add to dashboard Cite

Micro-RNAs (miRNAs) critically regulate several host defense mechanisms, but their roles in the bacteria-epithelium interplay remain unclear. Our results displayed that the expression of miR-155 and miR-23a were down-regulated in K. pneumoniae-infected pulmonary epithelial cells. The elevated bacterial adhesion on A549 cells followed the enhancement of the cellular levels of these two miRNAs. Meanwhile, a mechanistic study demonstrated that miR-155 promoted integrin α5β1 function and resulted in the increased actin polymerization. Moreover, a non-histone nuclear protein, high mobility group nucleosomal-binding domain 2 (HMGN2) served as the potential target of miR-155 and miR-23a to regulate the integrin α5β1 expression and K. pneumoniae adhesion. Furthermore, the expression of a known integrin transcription suppressor-Nuclear Factor-I (NFI) was also repressed by miR-155, which paralleled with its chromatin location in the promoter regions of integrin α5 and β1. These results uncover novel links between miRNAs and integrin function to regulate bacterial adhesion, indicating a potential mechanism of host cell autonomous immune response to K. pneumoniae infection.

show abstract

Section: Resultsmentioning

confidence: 99%

The modulation of MiR-155 and MiR-23a manipulates Klebsiella pneumoniae Adhesion on Human pulmonary Epithelial cells via Integrin α5β1 Signaling

Teng

Miao

Shen

et al. 2016

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Conversely, HMGA2 is able to bind directly to the twist1 [79,80]. HMGA2 is a known target of SUMOylation [81,82] that has been directly implicated in Xenopus EMT and migration of neural crest cells [83] as well as Xenopus cardiogenesis [84]. The different behavior of HMGA2 at the snai1 and twist1 promoters is reflected in the different effect of Gam1 on the expression of these two genes.…”

Section: Co--expression Analysismentioning

confidence: 99%

A Deficiency in SUMOylation Activity Disrupts Multiple Pathways Leading to Neural Tube and Heart Defects inXenopusEmbryos

Bertke

Dubiak

Cronin

et al. 2019

Preprint

View full text Add to dashboard Cite

show abstract

“…In order to further demonstrate the ability of DnSIZ1 to act as a SUMO E3 ligase, we generated pCDFDuet-1-Flag-DnSIZ1 and pCDFDuet-1-Flag-DnSIZ1 C380A constructs, in which the C380A mutation was introduced in its SP-RING, that is conserved in SIZ1s in different species and essential for SUMO ligase activity [ 45 ]. Then we performed SUMOylation assays in E.coli strain expressing DnSIZ1 together with AtSAE1a-SAE2, AtSCE1a and AtSUMO1 [ 59 , 60 ]. Compared with negative control, in the presence of AtSAE1a-SAE2, AtSCE1a and AtSUMO1, SUMOylation of DnSIZ1 was detected, indicating that DnSIZ1 can be sumoylated by E2 SUMO conjugation enzyme, which is a characteristic feature of SUMO E3 ligase (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Although we have established that key domains of DnSIZ1 are conserved in the AtSIZ1 protein, we wanted to further confirm that DnSIZ1 can function as a SUMO E3 ligase. Accordingly, we constructed a SUMOylation reactions system in E.coli [ 59 , 60 ] and demonstrated that DnSIZ1 is a functional SUMO E3 ligase (Fig. 10a, b ).…”

Section: Discussionmentioning

confidence: 99%

“…To reconstitute the SUMOylation system in vitro , pETSAE1a2 was co-transformed with pACYCDuet-AtSCE1-AtSUMO1 or pACYCDuet-AtSUMO1 into Escherichia coli BL21 (DE3) cells to generate competent cells [ 59 , 60 ]. For the SUMOylation reaction, the pCDFDuet-1-Flag-DnSIZ1 and pCDFDuet-1-Flag-DnSIZ1 C380A constructs were transformed into the above competent cells, respectively.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Functional characterization of DnSIZ1, a SIZ/PIAS-type SUMO E3 ligase from Dendrobium

Liu

Wang

et al. 2015

BMC Plant Biol

View full text Add to dashboard Cite

BackgroundSUMOylation is an important post-translational modification of eukaryotic proteins that involves the reversible conjugation of a small ubiquitin-related modifier (SUMO) polypeptide to its specific protein substrates, thereby regulating numerous complex cellular processes. The PIAS (protein inhibitor of activated signal transducers and activators of transcription [STAT]) and SIZ (scaffold attachment factor A/B/acinus/PIAS [SAP] and MIZ) proteins are SUMO E3 ligases that modulate SUMO conjugation. The characteristic features and SUMOylation mechanisms of SIZ1 protein in monocotyledon are poorly understood. Here, we examined the functions of a homolog of Arabidopsis SIZ1, a functional SIZ/PIAS-type SUMO E3 ligase from Dendrobium.ResultsIn Dendrobium, the predicted DnSIZ1 protein has domains that are highly conserved among SIZ/PIAS-type proteins. DnSIZ1 is widely expressed in Dendrobium organs and has a up-regulated trend by treatment with cold, high temperature and wounding. The DnSIZ1 protein localizes to the nucleus and shows SUMO E3 ligase activity when expressed in an Escherichia coli reconstitution system. Moreover, ectopic expression of DnSIZ1 in the Arabidopsis siz1-2 mutant partially complements several phenotypes and results in enhanced levels of SUMO conjugates in plants exposed to heat shock conditions. We observed that DnSIZ1 acts as a negative regulator of flowering transition which may be via a vernalization-induced pathway. In addition, ABA-hypersensitivity of siz1-2 seed germination can be partially suppressed by DnSIZ1.ConclusionsOur results suggest that DnSIZ1 is a functional homolog of the Arabidopsis SIZ1 with SUMO E3 ligase activity and may play an important role in the regulation of Dendrobium stress responses, flowering and development.Electronic supplementary materialThe online version of this article (doi:10.1186/s12870-015-0613-3) contains supplementary material, which is available to authorized users.

show abstract

High Mobility Group Nucleosomal Binding Domain 2 (HMGN2) SUMOylation by the SUMO E3 Ligase PIAS1 Decreases the Binding Affinity to Nucleosome Core Particles

Cited by 15 publications

References 42 publications

The modulation of MiR-155 and MiR-23a manipulates Klebsiella pneumoniae Adhesion on Human pulmonary Epithelial cells via Integrin α5β1 Signaling

The modulation of MiR-155 and MiR-23a manipulates Klebsiella pneumoniae Adhesion on Human pulmonary Epithelial cells via Integrin α5β1 Signaling

A Deficiency in SUMOylation Activity Disrupts Multiple Pathways Leading to Neural Tube and Heart Defects inXenopusEmbryos

Functional characterization of DnSIZ1, a SIZ/PIAS-type SUMO E3 ligase from Dendrobium

Contact Info

Product

Resources

About