BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae.

Nóbrega, Francisco G.; Nóbrega, Marina P.; Tzagoloff, Alexander

doi:10.1002/j.1460-2075.1992.tb05474.x

Cited by 154 publications

(127 citation statements)

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“…cerevisiae three homologues, BCS1, MSP1 (YTA4) and YME1 (YTA11), have been identified so far. BCS1 is required for the assembly of the ubiquinol-cytochrome c reductase complex [21]. The MSP1 (YTA4) gene product is an integral protein of the mitochondrial outer membrane and affects intramitochondrial protein sorting [22].…”

Section: Introductionmentioning

confidence: 99%

Yta10p is required for the ATP‐dependent degradation of polypeptides in the inner membrane of mitochondria

et al. 1994

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Incompletely synthesized polypeptides in the mitochondrial inner membrane are subject to rapid proteolysis. We demonstrate that Ytal 0p, a mitochondrial homologue of a conserved family of putative ATPases in Saccharomyces cerevisiae, is essential for this proteolytic process. Ytal0p-dependent degradation requires divalent metal ions and the hydrolysis of ATE Ytal0p is an integral protein of the inner mitochondrial membrane exposing the carboxy terminus to the mitochondrial matrix space. Based on the presence of consensus binding sites for ATE and for divalent metal ions found in a number of metal dependent endopeptidases, a direct role of Yta 10p in the proteolytic breakdown of membrane-associated polypeptides in mitochondria is suggested.

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Section: Introductionmentioning

confidence: 99%

Yta10p is required for the ATP‐dependent degradation of polypeptides in the inner membrane of mitochondria

et al. 1994

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“…Rhodanese (4) and 3-mercaptopyruvate sulfurtransferase (5) were effective in purified in vitro systems, comprising apoprotein, thiol, ferrous ion, and the respective sulfur-containing substrate, thiosulfate, or mercaptopyruvate. Analysis of yeast respiration-deficient mutants suggested a role for the BCS1 gene product (6) in the synthesis of functional Rieske protein. Studies on nif mutants of Azotobacter vinelandii (7) identified nifS as essential for nitrogenase activity.…”

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confidence: 99%

A Novel l-Cysteine/Cystine C-S-Lyase Directing [2Fe-2S] Cluster Formation of SynechocystisFerredoxin

Leibrecht

Kessler

1997

Journal of Biological Chemistry

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Iron-sulfur proteins acquire their clusters by posttranslational assembly. To identify components involved in this process an in vitro assay for holoprotein formation was established using the [2Fe-2S] ferredoxin of the cyanobacterium Synechocystis as a model. Conversion of apoferredoxin to the holo-form was observed in an anaerobic reaction medium containing Fe(NH 4 ) 2 (SO 4 ) 2 , L-cysteine, glutathione, and catalytic amounts of Synechocystis extract, specifically depleted of endogeneous ferredoxin. An approximate 2500-fold purification of the converter activity yielded a monomeric, 43-kDa, pyridoxal phosphate-containing enzyme, which catalyzed the breakdown of L-cysteine to yield sulfide (assembled in ferredoxin), pyruvate, and ammonia; 1 mol of [2Fe-2S] ferredoxin was formed per 2 mol of cysteine utilized.The purified enzyme also catalyzed the ␤-elimination reaction with cysteine in the absence of apoferredoxin. An increased reactivity was found with cystine instead of cysteine, which should yield cysteine persulfide as the primary product.These results provide a function-based identification of a cysteine/cystine C-S-lyase as a participant in ferredoxin Fe-S cluster formation. A substrate-derived cysteine persulfide could be involved in this reaction.Iron-sulfur (Fe-S) clusters are found as functional units in numerous electron-transferring proteins. They are essential in basic biological processes such as oxidative phosphorylation, photosynthesis, and nitrogen fixation. More recently, they have also been identified as components of enzymes not concerned with redox reactions (1). Lately they have been implicated in gene regulation (2).Despite these important and diverse functions and thorough biochemical investigations of Fe-S proteins, the biosynthetic steps leading to Fe-S cluster assembly have not been established. While it seems likely that enzyme-catalyzed reactions are involved in the formation of Fe-S clusters in vivo, the chemical reconstitution of apoproteins with free ferrous ion and sulfide in the presence of thiols (3) has been most intensively exploited for cluster build-up in vitro. Nevertheless, several proteins have been suggested as candidates in the biosynthetic process. Rhodanese (4) and 3-mercaptopyruvate sulfurtransferase (5) were effective in purified in vitro systems, comprising apoprotein, thiol, ferrous ion, and the respective sulfur-containing substrate, thiosulfate, or mercaptopyruvate. Analysis of yeast respiration-deficient mutants suggested a role for the BCS1 gene product (6) in the synthesis of functional Rieske protein. Studies on nif mutants of Azotobacter vinelandii (7) identified nifS as essential for nitrogenase activity. More recently, nifS was cloned and expressed in Escherichia coli; the gene product (NifS) was characterized as a pyridoxal phosphate-containing L-cysteine desulfurase, which yielded alanine and elemental sulfur as products (8); with dithiothreitol present in the reaction mixture, sulfide was produced instead of sulfur. Further work showed that the apo-...

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“…In addition it has been found (Tzagoloff and Dieckmann, 1990) that there are additional proteins that are needed for the proper functional assembly of these heteromeric membrane enzymes but these proteins are not part of the isolated biochemically active enzymes. These extra-enzyme activity factors are thought to be 'assembly facilitators' or specialized chaperones but the molecular mechanism of their action is usually unknown, although their inactivation generates clear respiratory deficient phenotypes (Nobrega et al, 1992;Souza et al, 2000). This class is mostly dispersed among NADH-cytochrome c reductase, cytochrome oxidase and general respiratory ability categories (Table III).…”

Section: Discussionmentioning

confidence: 99%

Sugarcane genes related to mitochondrial function

et al. 2001

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Mitochondria function as metabolic powerhouses by generating energy through oxidative phosphorylation and have become the focus of renewed interest due to progress in understanding the subtleties of their biogenesis and the discovery of the important roles which these organelles play in senescence, cell death and the assembly of iron-sulfur (Fe/S) centers. Using proteins from the yeast Saccharomyces cerevisiae, Homo sapiens and Arabidopsis thaliana we searched the sugarcane expressed sequence tag (SUCEST) database for the presence of expressed sequence tags (ESTs) with similarity to nuclear genes related to mitochondrial functions. Starting with 869 protein sequences, we searched for sugarcane EST counterparts to these proteins using the basic local alignment search tool TBLASTN similarity searching program run against 260,781 sugarcane ESTs contained in 81,223 clusters. We were able to recover 367 clusters likely to represent sugarcane orthologues of the corresponding genes from S. cerevisiae, H. sapiens and A. thaliana with E-value ≤ 10 -10 . Gene products belonging to all functional categories related to mitochondrial functions were found and this allowed us to produce an overview of the nuclear genes required for sugarcane mitochondrial biogenesis and function as well as providing a starting point for detailed analysis of sugarcane gene structure and physiology.

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BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae.

Cited by 154 publications

References 51 publications

Yta10p is required for the ATP‐dependent degradation of polypeptides in the inner membrane of mitochondria

Yta10p is required for the ATP‐dependent degradation of polypeptides in the inner membrane of mitochondria

A Novel l-Cysteine/Cystine C-S-Lyase Directing [2Fe-2S] Cluster Formation of SynechocystisFerredoxin

Sugarcane genes related to mitochondrial function

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