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Brassinosteroid Biosynthesis Is Modulated via a Transcription Factor Cascade of COG1, PIF4, and PIF5

Wei, Zhuoyun,Yuan, Tong,Tarkowsks&#x30c,a&#x301,, Danus&#x30c,e,Kim, Jeongsik,Nam, Hong Gil,Novs&#x30c,a&#x301,r&#x30c,a&#x301,k, Onds&#x30c,a&#x301,r&#x30c,ej,He, Kai,Gou, Xiaoping,Li, Jia American Society of Plant Biologists 2017 Plant Physiology Vol.174 No.2
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Brassinosteroids (BRs) are essential phytohormones regulating various developmental and physiological processes during normal growth and development. cog1-3D (cogwheel1-3D) was identified as an activation-tagged genetic modifier of bri1-5, an intermediate BR receptor mutant in Arabidopsis (Arabidopsis thaliana). COG1 encodes a Dof-type transcription factor found previously to act as a negative regulator of the phytochrome signaling pathway. cog1-3D single mutants show an elongated hypocotyl phenotype under light conditions. A loss-of-function mutant or inducible expression of a dominant negative form of COG1 in the wild type results in an opposite phenotype. A BR profile assay indicated that BR levels are elevated in cog1-3D seedlings. Quantitative reverse transcription-polymerase chain reaction analyses showed that several key BR biosynthetic genes are significantly up-regulated in cog1-3D compared with those of the wild type. Two basic helix-loop-helix transcription factors, PIF4 and PIF5, were found to be transcriptionally up-regulated in cog1-3D. Genetic analysis indicated that PIF4 and PIF5 were required for COG1 to promote BR biosynthesis and hypocotyl elongation. Chromatin immunoprecipitation and electrophoretic mobility shift assays indicated that COG1 binds to the promoter regions of PIF4 and PIF5, and PIF4 and PIF5 bind to the promoter regions of key BR biosynthetic genes, such as DWF4 and BR6ox2, to directly promote their expression. These results demonstrated that COG1 regulates BR biosynthesis via up-regulating the transcription of PIF4 and PIF5.
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Quest for Missing Proteins: Update 2015 on Chromosome-Centric Human Proteome Project

Horvatovich, Pe&#x301,ter,Lundberg, Emma K.,Chen, Yu-Ju,Sung, Ting-Yi,He, Fuchu,Nice, Edouard C.,Goode, Robert J.,Yu, Simon,Ranganathan, Shoba,Baker, Mark S.,Domont, Gilberto B.,Velasquez, Erika,Li, D American Chemical Society 2015 Journal of Proteome Research Vol.14 No.9
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This paper summarizes the recent activities of the Chromosome-Centric Human Proteome Project (C-HPP) consortium, which develops new technologies to identify yet-to-be annotated proteins (termed “missing proteins”) in biological samples that lack sufficient experimental evidence at the protein level for confident protein identification. The C-HPP also aims to identify new protein forms that may be caused by genetic variability, post-translational modifications, and alternative splicing. Proteogenomic data integration forms the basis of the C-HPP’s activities; therefore, we have summarized some of the key approaches and their roles in the project. We present new analytical technologies that improve the chemical space and lower detection limits coupled to bioinformatics tools and some publicly available resources that can be used to improve data analysis or support the development of analytical assays. Most of this paper’s content has been compiled from posters, slides, and discussions presented in the series of C-HPP workshops held during 2014. All data (posters, presentations) used are available at the C-HPP Wiki (<uri xlink:href='http://c-hpp.webhosting.rug.nl/' xlink:type='simple'>http://c-hpp.webhosting.rug.nl/</uri>) and in the Supporting Information.Graphic Abstract <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2015/jprobs.2015.14.issue-9/pr5013009/production/images/medium/pr-2014-013009_0005.gif'><A href='http://pubs.acs.org/doi/suppl/10.1021/pr5013009'>ACS Electronic Supporting Info</A>
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Multiple Redox Modes in the Reversible Lithiation of High-Capacity, Peierls-Distorted Vanadium Sulfide

Britto, Sylvia,Leskes, Michal,Hua, Xiao,Hé,bert, Claire-Alice,Shin, Hyeon Suk,Clarke, Simon,Borkiewicz, Olaf,Chapman, Karena W.,Seshadri, Ram,Cho, Jaephil,Grey, Clare P. American Chemical Society 2015 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY - Vol.137 No.26
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Vanadium sulfide VS4 in the patronite mineral structure is a linear chain compound comprising vanadium atoms coordinated by disulfide anions [S2]2–. 51V NMR shows that the material, despite having V formally in the d1 configuration, is diamagnetic, suggesting potential dimerization through metal–metal bonding associated with a Peierls distortion of the linear chains. This is supported by density functional calculations, and is also consistent with the observed alternation in V–V distances of 2.8 and 3.2 Å along the chains. Partial lithiation results in reduction of the disulfide ions to sulfide S2–, via an internal redox process whereby an electron from V4+ is transferred to [S2]2– resulting in oxidation of V4+ to V5+ and reduction of the [S2]2– to S2– to form Li3VS4 containing tetrahedral [VS4]3– anions. On further lithiation this is followed by reduction of the V5+ in Li3VS4 to form Li3+xVS4 (x = 0.5–1), a mixed valent V4+/V5+ compound. Eventually reduction to Li2S plus elemental V occurs. Despite the complex redox processes involving both the cation and the anion occurring in this material, the system is found to be partially reversible between 0 and 3 V. The unusual redox processes in this system are elucidated using a suite of short-range characterization tools including 51V nuclear magnetic resonance spectroscopy (NMR), S K-edge X-ray absorption near edge spectroscopy (XANES), and pair distribution function (PDF) analysis of X-ray data.Graphic Abstract <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/2015/jacsat.2015.137.issue-26/jacs.5b03395/production/images/medium/ja-2015-03395v_0013.gif'><A href='http://pubs.acs.org/doi/suppl/10.1021/ja5b03395'>ACS Electronic Supporting Info</A>

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