S
Sabeeha S. Merchant
Researcher at University of California, Berkeley
Publications - 231
Citations - 21730
Sabeeha S. Merchant is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Chlamydomonas reinhardtii & Chlamydomonas. The author has an hindex of 76, co-authored 215 publications receiving 18733 citations. Previous affiliations of Sabeeha S. Merchant include Lawrence Berkeley National Laboratory & California Institute for Quantitative Biosciences.
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Journal ArticleDOI
Genetic analysis of chloroplast c-type cytochrome assembly in Chlamydomonas reinhardtii: One chloroplast locus and at least four nuclear loci are required for heme attachment.
Zhiyi Xie,Duane Culler,Beth Welty Dreyfuss,Richard Kuras,Francis-André Wollman,Jacqueline Girard-Bascou,Sabeeha S. Merchant +6 more
TL;DR: It is concluded that the products of the CCS1-CCS4 loci are not required for translocation or processing of the preproteins but, like CcsA, they are required for the heme attachment step during assembly of both holocytochrome f and holocy tochrome c6.
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Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein.
TL;DR: A model where the WWD motif and histidine residues function in relaying heme from stroma to lumen is proposed and the existence of a cytochrome c assembly machinery containing CcsA, Ccs1 and additional components is postulated.
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FER1 and FER2 Encoding Two Ferritin Complexes in Chlamydomonas reinhardtii Chloroplasts Are Regulated by Iron
TL;DR: The Volvox genome contains orthologs of each FER gene, indicating that the duplication of FER genes and potential diversification of function occurred prior to the divergence of species in the Volvocales.
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The Elements of Plant Micronutrients
TL;DR: Amino acid R groups in proteins provide a limited repertoire of functional groups for catalyzing biochemical transformations, but the use of inorganic elements, particularly the first row transition metals, expands greatly the range of chemistry that can be catalyzed in a cell.
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Identification of Coq11, a New Coenzyme Q Biosynthetic Protein in the CoQ-Synthome in Saccharomyces cerevisiae
Christopher M. Allan,Agape M. Awad,Jarrett S. Johnson,Dyna I. Shirasaki,Charles Wang,Crysten E. Blaby-Haas,Sabeeha S. Merchant,Joseph A. Loo,Catherine F. Clarke +8 more
TL;DR: Discovery and characterization of yeast Coq biosynthetic proteins leads to an improved understanding of coenzyme Q biosynthesis and regulation and it is proposed that the open reading frame YLR290C be designated COQ11.