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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.


Structures of Arabidopsis thaliana LOV1 and LOV2 domains of phototropin 1 dark-adapted state. LOV1 domain (2Z6C; Nakasako et al., 2008), (A) and LOV2 of phototropin 1 in dark-adapted state (4HHD; Halavaty and Moffat, 2013), (B). Subunits B of LOV1 and LOV2 are shown in white, subunit A of the respective LOV domains is shown in colors according to secondary structure. Several α-helices (cyan) and β-strands (yellow) of the PAS core are labeled according to their nomenclature within the PAS domain as well as flanking helices, which are involved in dimerization and signaling. The Flavin mononucleotide chromophores (red) and the disulfide-bond-creating Cys at position 261 (Cys261, yellow) in the monomers of LOV2 domains, respectively, are depicted as sticks. C- and N-termini of subunits A and B are labeled (C, N). The graphic representation of the structure was generated using VMD (Humphrey et al., 1996).
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Figure 1: Structures of Arabidopsis thaliana LOV1 and LOV2 domains of phototropin 1 dark-adapted state. LOV1 domain (2Z6C; Nakasako et al., 2008), (A) and LOV2 of phototropin 1 in dark-adapted state (4HHD; Halavaty and Moffat, 2013), (B). Subunits B of LOV1 and LOV2 are shown in white, subunit A of the respective LOV domains is shown in colors according to secondary structure. Several α-helices (cyan) and β-strands (yellow) of the PAS core are labeled according to their nomenclature within the PAS domain as well as flanking helices, which are involved in dimerization and signaling. The Flavin mononucleotide chromophores (red) and the disulfide-bond-creating Cys at position 261 (Cys261, yellow) in the monomers of LOV2 domains, respectively, are depicted as sticks. C- and N-termini of subunits A and B are labeled (C, N). The graphic representation of the structure was generated using VMD (Humphrey et al., 1996).

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)

Structures of Arabidopsis thaliana LOV1 and LOV2 domains of phototropin 1 dark-adapted state. LOV1 domain (2Z6C; Nakasako et al., 2008), (A) and LOV2 of phototropin 1 in dark-adapted state (4HHD; Halavaty and Moffat, 2013), (B). Subunits B of LOV1 and LOV2 are shown in white, subunit A of the respective LOV domains is shown in colors according to secondary structure. Several α-helices (cyan) and β-strands (yellow) of the PAS core are labeled according to their nomenclature within the PAS domain as well as flanking helices, which are involved in dimerization and signaling. The Flavin mononucleotide chromophores (red) and the disulfide-bond-creating Cys at position 261 (Cys261, yellow) in the monomers of LOV2 domains, respectively, are depicted as sticks. C- and N-termini of subunits A and B are labeled (C, N). The graphic representation of the structure was generated using VMD (Humphrey et al., 1996).
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Figure 1: Structures of Arabidopsis thaliana LOV1 and LOV2 domains of phototropin 1 dark-adapted state. LOV1 domain (2Z6C; Nakasako et al., 2008), (A) and LOV2 of phototropin 1 in dark-adapted state (4HHD; Halavaty and Moffat, 2013), (B). Subunits B of LOV1 and LOV2 are shown in white, subunit A of the respective LOV domains is shown in colors according to secondary structure. Several α-helices (cyan) and β-strands (yellow) of the PAS core are labeled according to their nomenclature within the PAS domain as well as flanking helices, which are involved in dimerization and signaling. The Flavin mononucleotide chromophores (red) and the disulfide-bond-creating Cys at position 261 (Cys261, yellow) in the monomers of LOV2 domains, respectively, are depicted as sticks. C- and N-termini of subunits A and B are labeled (C, N). The graphic representation of the structure was generated using VMD (Humphrey et al., 1996).
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.