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ABSTRACT: The initiation of flowering in Arabidopsis is retarded or abolished by environmental stresses. Focusing on salt stress, we provide a molecular explanation for this well-known fact. A protein complex consisting of GI, a clock component important for flowering and SOS2, a kinase activating the [Na (+) ] antiporter SOS1, exists under no stress conditions. GI prevents SOS2 from activating SOS1. In the presence of NaCl, the SOS2/GI complex disintegrates and GI is degraded. SO2, together with the Ca ( 2+) -activated sensor of sodium ions, SOS3, activates SOS1. In gi mutants, SOS1 is constitutively activated and gi plants are more highly salt tolerant than wild type Arabidopsis. The model shows GI as a transitory regulator of SOS pathway activity whose presence or amount connects flowering to environmental conditions.
Plant signaling & behavior 05/2013; 8(7).
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Woe-Yeon Kim,
Zahir Ali, Hee Jin Park,
Su Jung Park,
Joon-Yung Cha,
Javier Perez-Hormaeche,
Francisco Javier Quintero,
Gilok Shin,
Mi Ri Kim,
Zhang Qiang,
Li Ning,
Hyeong Cheol Park,
Sang Yeol Lee,
Ray A Bressan,
Jose M Pardo,
Hans J Bohnert,
Dae-Jin Yun
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ABSTRACT: Environmental challenges to plants typically entail retardation of vegetative growth and delay or cessation of flowering. Here we report a link between the flowering time regulator, GIGANTEA (GI), and adaptation to salt stress that is mechanistically based on GI degradation under saline conditions, thus retarding flowering. GI, a switch in photoperiodicity and circadian clock control, and the SNF1-related protein kinase SOS2 functionally interact. In the absence of stress, the GI:SOS2 complex prevents SOS2-based activation of SOS1, the major plant Na(+)/H(+)-antiporter mediating adaptation to salinity. GI overexpressing, rapidly flowering, plants show enhanced salt sensitivity, whereas gi mutants exhibit enhanced salt tolerance and delayed flowering. Salt-induced degradation of GI confers salt tolerance by the release of the SOS2 kinase. The GI-SOS2 interaction introduces a higher order regulatory circuit that can explain in molecular terms, the long observed connection between floral transition and adaptive environmental stress tolerance in Arabidopsis.
Nature Communications 01/2013; 4:1352. · 7.40 Impact Factor
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ABSTRACT: Small ubiquitin-like modifier (SUMO) is a small (∼12kDa) protein that occurs in all eukaryotes and participates in the reversible posttranslational modification of target cellular proteins. The three-dimensional structure of SUMO and ubiquitin (Ub) are superimposable although there is very little similarity in their primary amino acid sequences. In all organisms, conjugation and deconjugation of Ub and SUMO proceed by the same reactions while using pathway-specific enzymes. SUMO conjugation in plants is a part of the controls governing important biological processes such as growth, development, flowering, environmental (abiotic) stress responses, and response to pathogen infection. Most of the evidence for this comes from genetic analyses. Recent efforts to dissect the function of sumoylation have focused on uncovering targets of SUMO conjugation by using either a yeast two-hybrid screen employing components of the SUMO cycle as bait or by using affinity purification of SUMO-conjugated proteins followed by identification of these proteins by mass spectrometry. This chapter reviews the current knowledge regarding sumoylation in plants, with special focus on the model plant Arabidopsis thaliana.
International review of cell and molecular biology 01/2013; 300C:161-209. · 4.48 Impact Factor
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ABSTRACT: Posttranslational modifications of proteins by small polypeptides including ubiquitination, neddylation (related to ubiquitin
(RUB) conjugation), and sumoylation are implicated in plant growth and development, and they regulate protein degradation,
location, and interaction with other proteins. Ubiquitination mediates the selective degradation of proteins by the ubiquitin
(Ub)/proteasome pathway. The ubiquitin-like protein RUB is conjugated to cullins, which are part of a ubiquitin E3 ligase
complex that is involved in auxin hormonal signaling. Sumoylation, by contrast, is known for its involvement in guiding protein
interactions related to abiotic and biotic stresses and in the regulation of flowering time. ATG8/ATG12-mediated autophagy
influences degradation and recycling of cellular components. Other ubiquitin-like modifiers (ULPs) such as homology to Ub-1,
ubiquitin-fold modifier 1, and membrane-anchored Ub-fold are also found in Arabidopsis. ULPs share similar three-dimensional structures and a conjugation system, including E1 activating enzymes, E2 conjugation
enzymes, and E3 ligases, as well as proteases for deconjugation and recycling of the tags. However, each of the ULP posttranslational
modifications possesses its own specific enzymes and modifies its specific targets selectively. This review discusses recent
findings on ubiquitination and ubiquitin-like modifier processes and their roles in the posttranslational modification of
proteins in Arabidopsis.
Keywords
Arabidopsis
–Posttranslational modification–Ubiquitination–Ubiquitin-like modifiers
Journal of Plant Biology 04/2012; 54(5):275-285. · 1.07 Impact Factor
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ABSTRACT: The traditional focus on the central dogma of molecular biology, from gene through RNA to protein, has now been replaced by the recognition of an additional mechanism. The new regulatory mechanism, post-translational modifications to proteins, can actively alter protein function or activity introducing additional levels of functional complexity by altering cellular and sub-cellular location, protein interactions and the outcome of biochemical reaction chains. Modifications by ubiquitin (Ub) and ubiquitin-like modifiers systems are conserved in all eukaryotic organisms. One of them, small ubiquitin-like modifier (SUMO) is present in plants. The SUMO mechanism includes several isoforms of proteins that are involved in reactions of sumoylation and de-sumoylation. Sumoylation affects several important processes in plants. Outstanding among those are responses to environmental stresses. These may be abiotic stresses, such as phosphate deficiency, heat, low temperature, and drought, or biotic stressses, as well including defense reactions to pathogen infection. Also, the regulations of flowering time, cell growth and development, and nitrogen assimilation have recently been added to this list. Identification of SUMO targets is material to characterize the function of sumoylation or desumoylation. Affinity purification and mass spectrometric identification have been done lately in plants. Further SUMO noncovalent binding appears to have function in other model organisms and SUMO interacting proteins in plants will be of interest to plant biologists who dissect the dynamic function of SUMO. This review will discuss results of recent insights into the role of sumoylation in plants.
Molecules and Cells 09/2011; 32(4):305-16. · 2.18 Impact Factor
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Hyeong Cheol Park,
Wonkyun Choi, Hee Jin Park,
Mi Sun Cheong,
Yoon Duck Koo,
Gilok Shin,
Woo Sik Chung,
Woe-Yeon Kim,
Min Gab Kim,
Ray A Bressan,
Hans J Bohnert,
Sang Yeol Lee,
Dae-Jin Yun
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ABSTRACT: Reversible conjugation of the small ubiquitin modifier (SUMO) peptide to proteins (SUMOylation) plays important roles in cellular processes in animals and yeasts. However, little is known about plant SUMO targets. To identify SUMO substrates in Arabidopsis and to probe for biological functions of SUMO proteins, we constructed 6xHis-3xFLAG fused AtSUMO1 (HFAtSUMO1) controlled by the CaMV35S promoter for transformation into Arabidopsis Col-0. After heat treatment, an increased sumoylation pattern was detected in the transgenic plants. SUMO1-modified proteins were selected after two-dimensional gel electrophoresis (2-DE) image analysis and identified using matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). We identified 27 proteins involved in a variety of processes such as nucleic acid metabolism, signaling, metabolism, and including proteins of unknown functions. Binding and sumoylation patterns were confirmed independently. Surprisingly, MCM3 (At5G46280), a DNA replication licensing factor, only interacted with and became sumoylated by AtSUMO1, but not by SUMO1ΔGG or AtSUMO3. The results suggest specific interactions between sumoylation targets and particular sumoylation enzymes.
Molecules and Cells 05/2011; 32(2):143-51. · 2.18 Impact Factor
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Hyeong Cheol Park,
Hun Kim,
Sung Cheol Koo, Hee Jin Park,
Mi Sun Cheong,
Hyewon Hong,
Dongwon Baek,
Woo Sik Chung,
Doh Hoon Kim,
Ray A Bressan,
Sang Yeol Lee,
Hans J Bohnert,
Dae-Jin Yun
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ABSTRACT: Sumoylation is a post-translational regulatory process in diverse cellular processes in eukaryotes, involving conjugation/deconjugation of small ubiquitin-like modifier (SUMO) proteins to other proteins thus modifying their function. The PIAS [protein inhibitor of activated signal transducers and activators of transcription (STAT)] and SAP (scaffold attachment factor A/B/acinus/PIAS)/MIZ (SIZ) proteins exhibit SUMO E3-ligase activity that facilitates the conjugation of SUMO proteins to target substrates. Here, we report the isolation and molecular characterization of Oryza sativa SIZ1 (OsSIZ1) and SIZ2 (OsSIZ2), rice homologs of Arabidopsis SIZ1. The rice SIZ proteins are localized to the nucleus and showed sumoylation activities in a tobacco system. Our analysis showed increased amounts of SUMO conjugates associated with environmental stresses such as high and low temperature, NaCl and abscisic acid (ABA) in rice plants. The expression of OsSIZ1 and OsSIZ2 in siz1-2 Arabidopsis plants partially complemented the morphological mutant phenotype and enhanced levels of SUMO conjugates under heat shock conditions. In addition, ABA-hypersensitivity of siz1-2 seed germination was partially suppressed by OsSIZ1 and OsSIZ2. The results suggest that rice SIZ1 and SIZ2 are able to functionally complement Arabidopsis SIZ1 in the SUMO conjugation pathway. Their effects on the Arabidopsis mutant suggest a function for these genes related to stress responses and stress adaptation.
Plant Cell and Environment 11/2010; 33(11):1923-34. · 5.22 Impact Factor
