The nucleotide sequence of Saccharomyces cerevisiae chromosome IV

Jacq, C.; Alt-Mörbe, J.; André, Brunó; Arnold, Walter; Bahr, A.; Ballesta, J. P. G.; Bargues, Marìa Dolores; Baron, L.; Becker, Anke; Biteau, N.; Blöcker, H.; Blugeon, C.; Boskovic, Jasminka; Brandt, P.; Brückner, Margit; Buitrago, María J.; Coster, Françoise; Delaveau, T.; Rey, Francisco del; Dujon, Bernard; Eide, L. G.; García-Cantalejo, Jesús; Goffeau, André; Gomez-Peris, A.; Granotier, C.; Hanemann, V.; Hankeln, Thomas; Hoheisel, Jöerg; Jäger, W.; Jiménez, Alberto; Jonniaux, Jean-Luc; Krämer, Christian; Küster, H.; Laamanen, Päivi; Legros, Y.; Louis, Edward J.; Möller-Rieker, Sabine; Monnet, A.; Moro, M.; Müller-Auer, S.; Nussbaumer, B; Paricio, Nuria; Paulin, L.; Perea, J.; Pérez-Alonso, Manuel; Pérez‐Ortín, José E.; Pohl, Thomas; Prydz, H.; Purnelle, Bénédicte; Rasmussen, Søren W.; Remacha, Miguel; Revuelta, José Luis; Rieger, Michael A.; Salom, David; Saluz, Hans Peter; Saiz, Julia E.; Sarén, Ari-Matti; Schäfer, Melanie; Scharfe, M.; Schmidt, Edith; Schneider, Claudio; Scholler, Patrik; Schwarz, Sylvia E.; Soler-mira, Aida; Urrestarazu, L. A.; Verhasselt, Peter; Vissers, Stéphan; Voet, Martine; Volckaert, Guido; Wagner, G.; Wambutt, R.; Wedler, E.; Wedler, H.; Wölfl, S.; Harris, David; Bowman, Sharen; Brown, D.; Churcher, Carol; Connor, R.; Dedman, K.; Gentles, S.; Hamlin, N.; Hunt, Sarah; Jones, Louis; McDonald, Sarah; Murphy, Lee; Niblett, David; Odell, C.; Oliver, Karen; Rajandream, Marie Adèle; Richards, C.; Shore, L.; Walsh, Sean; Barrell, Bart; Dietrich, Fred S.; Mulligan, John T.; Allen, Elizabeth; Araujo, R.; Aviles, E.; Berno, Anthony; Carpenter, J.; Chen, E.; Cherry, J. Michael; Chung, Esther K.; Duncan, Michael; Hunicke-Smith, Scott Patrick; Hyman, Richard W.; Komp, Caridad; Lashkari, Deval; Lew, H.; Lin, David C.; Mosedale, D.; Nakahara, K.; Namath, Allen; Oefner, Peter J.; Oh, Chi Eun; Petel, Fabien; Roberts, Dorothy B.; Schramm, S.; Schroeder, Matthew; Shogren, T.; Shroff, N.; Winant, A.; Yelton, M. Melanie; Botstein, David; Davis, Ron; Johnston, Mark; Hillier, L.; Riles, Linda; Albermann, Kaj; Hani, Jean; Heumann, Klaus G.; Kleine, K.; Mewes, Hans‐Werner; Zollner, Alfred; Zaccaria, Paolo

doi:10.1038/387s075

Cited by 82 publications

(44 citation statements)

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“…Locus YDR373w on chromosome IV (ref. 20) was dubbed FRQ1 because it encodes a 190-residue protein with highest relatedness (60% identity) to frequenin (Fig. 1a).…”

Section: Resultsmentioning

confidence: 99%

Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol-4-OH kinase

et al. 1999

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In metazoans, certain calmodulin-related calcium-binding proteins (recoverins, neurocalcins and frequenins) are found at highest levels in excitable cells, but their physiological roles are largely uncharacterized. Here we show that Saccharomyces cerevisiae contains a frequenin homologue, Frq1, and that its target is Pik1, a phosphatidylinositol-4-OH kinase. Frq1 binds to a conserved sequence motif in Pik1 outside Pik1's catalytic domain and stimulates its activity in vitro. N-myristoylated Frq1 may also assist in Pik1 localization.

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“…Locus YDR373w on chromosome IV (ref. 20) was dubbed FRQ1 because it encodes a 190-residue protein with highest relatedness (60% identity) to frequenin (Fig. 1a).…”

Section: Resultsmentioning

confidence: 99%

Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol-4-OH kinase

et al. 1999

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“…Furthermore, it has been shown that the N-terminal half of the SANT domain is required for interactions with histone acetyltransferases or histone deacetylases, while the C-terminal half is required for the interaction with chromatin [30], [31], [32]. Although the amino acid identity of the SANT domains between PIE1 and other proteins, including DOMINO [16], SRCAP [17], and SWR1 from yeast [15], is very low, we found that the conserved and functionally important residues of the SANT domain are still present in this region for the PIE1 orthologs (Figure S1; see also [19]). Additionally, like PIE1, OsPIE1 has a unique 11-amino acid linker, GGAF(AGGA for PIE1) YRGRYRHP), between the N-terminal and C-terminal halves of the SANT domain (Figure S1).…”

Section: Resultsmentioning

confidence: 99%

“…The catalytic subunit of these complexes is Swr1 in yeast [12], [15], Domino in Drosophila [13], [16], SRCAP in humans [17], [18], and PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1 (PIE1) in Arabidopsis [4], [5], [19]. These proteins contain an ATPase domain and belong to the SNF2 family of chromatin remodeling factors.…”

Section: Introductionmentioning

confidence: 99%

OsPIE1, the Rice Ortholog of Arabidopsis PHOTOPERIOD-INDEPENDENT EARLY FLOWERING1, Is Essential for Embryo Development

Deng

JianFei

et al. 2010

PLoS ONE

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BackgroundThe SWR1 complex is important for the deposition of histone variant H2A.Z into chromatin necessary to robustly regulate gene expression during growth and development. In Arabidopsis thaliana, the catalytic subunit of the SWR1-like complex, encoded by PIE1 (PHOTOPERIOD-INDEPENDENT EARLY FLOWERING1), has been shown to function in multiple developmental processes including flowering time pathways and petal number regulation. However, the function of the PIE1 orthologs in monocots remains unknown.Methodology/FindingsWe report the identification of the rice (Oryza sativa) ortholog, OsPIE1. Although OsPIE1 does not exhibit a conserved exon/intron structure as Arabidopsis PIE1, its encoded protein is highly similar to PIE1, sharing 53.9% amino acid sequence identity. OsPIE1 also has a very similar expression pattern as PIE1. Furthermore, transgenic expression of OsPIE1 completely rescued both early flowering and extra petal number phenotypes of the Arabidopsis pie1-2 mutant. However, homozygous T-DNA insertional mutants of OsPIE1 in rice were embryonically lethal, in contrast to the viable mutants in the orthologous genes for yeast, Drosophila and Arabidopsis (Swr1, DOMINO and PIE1, respectively).Conclusions/SignificanceTaken together, our results suggest that OsPIE1 is the rice ortholog of Arabidopsis PIE1 and plays an essential role in rice embryo development.

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“…Recently, the complete genome of Saccharomyces cerevisiae was analyzed by several groups (Oliver et al 1992;Dojon et al 1994Dojon et al , 1997Feldman et al 1994;Johnston et al 1994Johnston et al , 1997Bussey et al 1995Bussey et al , 1997Murakami et al 1995;Galibert et al 1996;Goffeau et al 1996;Bowman et al 1997;Churcher et al 1997;Dietrich et al 1997;Jacq et Philippsen et al 1997;Tettelin et al 1997). We used their data from GenomeNet (http://www.genome.ad.jp) and analyzed them with a personal computer.…”

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confidence: 99%

Gene assembly consisting of small units with similar amino acid composition in the Saccharomyces cerevisiae genome

Sorimachi

Okayasu

2003

Mycoscience

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Amino acid compositions of all genes in Saccharomyces cerevisiae were determined using a computer analysis of the complete genome. The amino acid composition of an assembly of several genes or a single gene consisted of 3000-7000 amino acid residues forming a certain pattern of amino acid composition. This rule was independent not only of the gene size, but also of the gene position. Thus, the small units, consisting of 3000-7000 amino acid residues, showed a similar amino acid composition, and they formed all the genes in the complete genome.

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The nucleotide sequence of Saccharomyces cerevisiae chromosome IV

Cited by 82 publications

References 0 publications

Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol-4-OH kinase

Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol-4-OH kinase

OsPIE1, the Rice Ortholog of Arabidopsis PHOTOPERIOD-INDEPENDENT EARLY FLOWERING1, Is Essential for Embryo Development

Gene assembly consisting of small units with similar amino acid composition in the Saccharomyces cerevisiae genome

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