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Setting the PAS, the role of circadian PAS domain proteins during environmental adaptation in plants.

Vogt JH, Schippers JH - Front Plant Sci (2015)

Bottom Line: The per-ARNT-sim (PAS) domain represents an ancient protein module that can be found across all kingdoms of life.In plants, several PAS domain-containing proteins form an integral part of the circadian clock and regulate responses to environmental change.Here, we discuss the role of PAS domain-containing proteins in anticipation, and adaptation to environmental changes in plants.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biochemistry and Biology, University of Potsdam , Potsdam, Germany.

ABSTRACT
The per-ARNT-sim (PAS) domain represents an ancient protein module that can be found across all kingdoms of life. The domain functions as a sensing unit for a diverse array of signals, including molecular oxygen, small metabolites, and light. In plants, several PAS domain-containing proteins form an integral part of the circadian clock and regulate responses to environmental change. Moreover, these proteins function in pathways that control development and plant stress adaptation responses. Here, we discuss the role of PAS domain-containing proteins in anticipation, and adaptation to environmental changes in plants.

No MeSH data available.


Composition of PAS containing multidomain proteins in plants. Schematic representation of PAS domain-containing proteins in Arabidopsis and their multidomain architecture (Mitchell et al., 2015). The PAS module is located in variable positions within the protein and associated with a variety of effector domains. Abbreviations: PAS, per-arnt-sim domain; PASLOV1/2, LOV (light oxygen, or voltage) subclass of PAS domain; PASMEKHLA, PAS-like MEKHLA domain; S/T kinase, Serine/Threonine kinase; F-BOX, domain interacting with SCF complex; KELCH, KELCH repeat; GAF, cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA; PHY, GAF-like domain/Chromobillin binding; START, StAR-related lipid-transfer; HD-SAD, HD-START-associated domain; HD, homeodomain; LZ, Leucine zipper; aa, amino acids.
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Figure 2: Composition of PAS containing multidomain proteins in plants. Schematic representation of PAS domain-containing proteins in Arabidopsis and their multidomain architecture (Mitchell et al., 2015). The PAS module is located in variable positions within the protein and associated with a variety of effector domains. Abbreviations: PAS, per-arnt-sim domain; PASLOV1/2, LOV (light oxygen, or voltage) subclass of PAS domain; PASMEKHLA, PAS-like MEKHLA domain; S/T kinase, Serine/Threonine kinase; F-BOX, domain interacting with SCF complex; KELCH, KELCH repeat; GAF, cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA; PHY, GAF-like domain/Chromobillin binding; START, StAR-related lipid-transfer; HD-SAD, HD-START-associated domain; HD, homeodomain; LZ, Leucine zipper; aa, amino acids.

Mentions: The PAS domain is a sensory and protein–protein-interaction module, which can be found throughout all kingdoms of life. It was originally identified by sequence homology of three eukaryotic proteins: the circadian protein Period (per) and developmental regulator Sim (single-minded) of Drosophila and the vertebrate aryl hydrocarbon receptor nuclear transporter (ARNT), which comprise two PAS motifs each (Nambu et al., 1991). Conserved residues C-terminal to the PAS motif were at first assigned as PAC motif (Ponting and Aravind, 1997). However, the first three-dimensional structure of the PAS domain revealed that both, the PAS and PAC motif, form a globular fold made up of about 100 residues, thus redefining the PAS domain (Hefti et al., 2004). Although PAS domains share only a low sequence homology on the amino acid level (∼20%), the three-dimensional structure is highly conserved (Mei and Dvornyk, 2014). The PAS fold consists of an antiparallel five-stranded β-sheet in topological order 2-1-5-4-3 and several flanking α-helices (Figure 1), which are either packed on the core or extend from it (Möglich et al., 2009). In plants, PAS domains are combined in multidomain proteins with functionally diverse effector/regulatory domains such as Serine/Threonine kinases, F-Boxes or, HD-ZIP domains (Figure 2 and Table 1), thus mediating a plethora of cellular responses. Interestingly, the phytochrome and F-BOX containing PAS domain proteins were shown to interact (Jarillo et al., 2001a; Kim et al., 2007) and function either as an input to the clock and/or an integral component of the circadian oscillator.


Setting the PAS, the role of circadian PAS domain proteins during environmental adaptation in plants.

Vogt JH, Schippers JH - Front Plant Sci (2015)

Composition of PAS containing multidomain proteins in plants. Schematic representation of PAS domain-containing proteins in Arabidopsis and their multidomain architecture (Mitchell et al., 2015). The PAS module is located in variable positions within the protein and associated with a variety of effector domains. Abbreviations: PAS, per-arnt-sim domain; PASLOV1/2, LOV (light oxygen, or voltage) subclass of PAS domain; PASMEKHLA, PAS-like MEKHLA domain; S/T kinase, Serine/Threonine kinase; F-BOX, domain interacting with SCF complex; KELCH, KELCH repeat; GAF, cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA; PHY, GAF-like domain/Chromobillin binding; START, StAR-related lipid-transfer; HD-SAD, HD-START-associated domain; HD, homeodomain; LZ, Leucine zipper; aa, amino acids.
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Related In: Results  -  Collection

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Show All Figures
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Figure 2: Composition of PAS containing multidomain proteins in plants. Schematic representation of PAS domain-containing proteins in Arabidopsis and their multidomain architecture (Mitchell et al., 2015). The PAS module is located in variable positions within the protein and associated with a variety of effector domains. Abbreviations: PAS, per-arnt-sim domain; PASLOV1/2, LOV (light oxygen, or voltage) subclass of PAS domain; PASMEKHLA, PAS-like MEKHLA domain; S/T kinase, Serine/Threonine kinase; F-BOX, domain interacting with SCF complex; KELCH, KELCH repeat; GAF, cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA; PHY, GAF-like domain/Chromobillin binding; START, StAR-related lipid-transfer; HD-SAD, HD-START-associated domain; HD, homeodomain; LZ, Leucine zipper; aa, amino acids.
Mentions: The PAS domain is a sensory and protein–protein-interaction module, which can be found throughout all kingdoms of life. It was originally identified by sequence homology of three eukaryotic proteins: the circadian protein Period (per) and developmental regulator Sim (single-minded) of Drosophila and the vertebrate aryl hydrocarbon receptor nuclear transporter (ARNT), which comprise two PAS motifs each (Nambu et al., 1991). Conserved residues C-terminal to the PAS motif were at first assigned as PAC motif (Ponting and Aravind, 1997). However, the first three-dimensional structure of the PAS domain revealed that both, the PAS and PAC motif, form a globular fold made up of about 100 residues, thus redefining the PAS domain (Hefti et al., 2004). Although PAS domains share only a low sequence homology on the amino acid level (∼20%), the three-dimensional structure is highly conserved (Mei and Dvornyk, 2014). The PAS fold consists of an antiparallel five-stranded β-sheet in topological order 2-1-5-4-3 and several flanking α-helices (Figure 1), which are either packed on the core or extend from it (Möglich et al., 2009). In plants, PAS domains are combined in multidomain proteins with functionally diverse effector/regulatory domains such as Serine/Threonine kinases, F-Boxes or, HD-ZIP domains (Figure 2 and Table 1), thus mediating a plethora of cellular responses. Interestingly, the phytochrome and F-BOX containing PAS domain proteins were shown to interact (Jarillo et al., 2001a; Kim et al., 2007) and function either as an input to the clock and/or an integral component of the circadian oscillator.

Bottom Line: The per-ARNT-sim (PAS) domain represents an ancient protein module that can be found across all kingdoms of life.In plants, several PAS domain-containing proteins form an integral part of the circadian clock and regulate responses to environmental change.Here, we discuss the role of PAS domain-containing proteins in anticipation, and adaptation to environmental changes in plants.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biochemistry and Biology, University of Potsdam , Potsdam, Germany.

ABSTRACT
The per-ARNT-sim (PAS) domain represents an ancient protein module that can be found across all kingdoms of life. The domain functions as a sensing unit for a diverse array of signals, including molecular oxygen, small metabolites, and light. In plants, several PAS domain-containing proteins form an integral part of the circadian clock and regulate responses to environmental change. Moreover, these proteins function in pathways that control development and plant stress adaptation responses. Here, we discuss the role of PAS domain-containing proteins in anticipation, and adaptation to environmental changes in plants.

No MeSH data available.