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Phosphoprotein SAK1 is a regulator of acclimation to singlet oxygen in Chlamydomonas reinhardtii.

Wakao S, Chin BL, Ledford HK, Dent RM, Casero D, Pellegrini M, Merchant SS, Niyogi KK - Elife (2014)

Bottom Line: The unicellular green alga Chlamydomonas reinhardtii is capable of acclimating specifically to singlet oxygen stress, but the retrograde signaling pathway from the chloroplast to the nucleus mediating this response is unknown.Analysis of genome-wide changes in RNA abundance during acclimation to singlet oxygen revealed that SAK1 is a key regulator of the gene expression response during acclimation.The SAK1 gene encodes an uncharacterized protein with a domain conserved among chlorophytes and present in some bZIP transcription factors.

View Article: PubMed Central - PubMed

Affiliation: Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, United States.

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Secondary structure prediction of SAK1 domain.SAK1 domain modeled against its best-hit nickel cobalt resistance protein cnrr by PHYRE. 44% (coverage) of the SAK1 domain was aligned with 73.6% confidence.DOI:http://dx.doi.org/10.7554/eLife.02286.018
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fig5s2: Secondary structure prediction of SAK1 domain.SAK1 domain modeled against its best-hit nickel cobalt resistance protein cnrr by PHYRE. 44% (coverage) of the SAK1 domain was aligned with 73.6% confidence.DOI:http://dx.doi.org/10.7554/eLife.02286.018

Mentions: Amino acid positions 900 to 1089 of SAK1, corresponding to the region aligned with other proteins in Figure 5—figure supplement 1, were searched for secondary structure using PHYRE, and this region was predicted to consist of mostly alpha helices with some disordered intervals. The top hit was a cobalt/nickel-binding resistance protein cnrr, and 44% of the residues were modeled with 73.6% confidence (Figure 5—figure supplement 2).


Phosphoprotein SAK1 is a regulator of acclimation to singlet oxygen in Chlamydomonas reinhardtii.

Wakao S, Chin BL, Ledford HK, Dent RM, Casero D, Pellegrini M, Merchant SS, Niyogi KK - Elife (2014)

Secondary structure prediction of SAK1 domain.SAK1 domain modeled against its best-hit nickel cobalt resistance protein cnrr by PHYRE. 44% (coverage) of the SAK1 domain was aligned with 73.6% confidence.DOI:http://dx.doi.org/10.7554/eLife.02286.018
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4067076&req=5

fig5s2: Secondary structure prediction of SAK1 domain.SAK1 domain modeled against its best-hit nickel cobalt resistance protein cnrr by PHYRE. 44% (coverage) of the SAK1 domain was aligned with 73.6% confidence.DOI:http://dx.doi.org/10.7554/eLife.02286.018
Mentions: Amino acid positions 900 to 1089 of SAK1, corresponding to the region aligned with other proteins in Figure 5—figure supplement 1, were searched for secondary structure using PHYRE, and this region was predicted to consist of mostly alpha helices with some disordered intervals. The top hit was a cobalt/nickel-binding resistance protein cnrr, and 44% of the residues were modeled with 73.6% confidence (Figure 5—figure supplement 2).

Bottom Line: The unicellular green alga Chlamydomonas reinhardtii is capable of acclimating specifically to singlet oxygen stress, but the retrograde signaling pathway from the chloroplast to the nucleus mediating this response is unknown.Analysis of genome-wide changes in RNA abundance during acclimation to singlet oxygen revealed that SAK1 is a key regulator of the gene expression response during acclimation.The SAK1 gene encodes an uncharacterized protein with a domain conserved among chlorophytes and present in some bZIP transcription factors.

View Article: PubMed Central - PubMed

Affiliation: Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, United States.

Show MeSH
Related in: MedlinePlus