浜у搧璧勮 > 閰墊瘝鑿岃〃杈捐氨鑺墖 Yeast OneArrayR v1

 
  Yeast microarray for gene expression   閰墊瘝鑿岃〃杈捐氨鑺墖 v1 鐨勬帰閽堟槸閲囩敤 Operon Yeast Genome Array-Ready Oligo Set (AROS) v1.1 涓?Yeast Brown Lab Oligo Extension (YBOX) v1.0 鎺㈤拡緇勮祫璁墍璁捐錛?涓洪暱閾?70 涓⒈鍩哄鏍擱吀鎺㈤拡銆?閰墊瘝鑿岃〃杈捐氨鑺墖 v1 浜?2010 騫?3 鏈堜笂甯傘€?鎺㈤拡鐨嗚璁″湪紱?3鈥?/font> 绔?750 紕卞熀浠ュ唴鐨勫簭鍒楋紝閫傚悎鐢ㄦ潵榪涜鍩哄洜琛ㄧ幇鐨勭爺絀躲€?

 
 
 
閰墊瘝鑿岃〃杈捐氨鑺墖 v1 鎺㈤拡鍐呭
鎺㈤拡縐嶇被 鎺㈤拡鏁?/font>
  鍩哄洜鎺㈤拡璁捐璧勬枡搴擄細 6,958
          - Operon Yeast Genome Array-Ready Oligo Set (AROS) v1.1
          - Yeast Brown Lab Oligo Extension (YBOX) v1.0
  鎺у埗鎺㈤拡鏁?/font> 684
  鎬繪帰閽堟暟 7,642


  鍩?鍥?鎺?閽?/b>

閰墊瘝鑿岃〃杈捐氨鑺墖 v1 鏄敱鍗庤仈鐨勬妧鏈洟闃熶笌涓ぎ鐮旂┒闄㈡墍鍏卞悓鍚堜綔鐢熶駭錛?鎺㈤拡鐨勮璁″強鏀墮泦鏄弬鑰冨浗闄呬笂杈冩櫘閬嶄嬌鐢ㄧ殑 Operon Yeast Genome Array-Ready Oligo Set (AROS) v1.1 涓?Yeast Brown Lab Oligo Extension (YBOX) v1.0 鐨勬帰閽堢粍璧勮錛?甯冩斁 70 涓⒈鍩哄鏍擱吀鐨勯暱閾炬帰閽堛€?鎵€鏈夌殑鎺㈤拡鐨嗗垎甯冨湪紱誨熀鍥?3鈥?绔?750 紕卞熀浠ュ唴鐨勫簭鍒楋紝 閫傚悎鐢ㄦ潵榪涜鍩哄洜琛ㄧ幇鐨勭爺絀躲€? 澶ч紶琛ㄨ揪璋辮姱鐗囨槸鍙傝€冨浗闄呭叕璁や箣 RefSeq 鍙?Ensembl 搴忓垪璧勬枡搴擄紝 璁捐闀塊摼 60 涓⒈鍩哄鏍擱吀 (sense-strand) 鐨勫熀鍥犳帰閽堬紝 鍐呭涓昏浠ヨ泲鐧借川緙栫爜鍩哄洜 (protein-coding gene) 涓轟富錛?鎻愪緵楂樺熀鍥犺鐩栫巼騫朵笖姣忎竴涓帰閽堝鍏舵潵婧愯祫鏂欏簱鐨勭洰鏍囧熀鍥犵殕鍏烽珮搴︿笓涓€鎬э紝閬垮厤闈炵洰鏍囧熀鍥犵殑鏉備氦褰卞搷銆?



  鎺?鍒?鎺?閽?/b>

涓虹‘淇濊姱鐗囨暟鎹搧璐紝鍗庤仈鎶€鏈洟闃熺粡榪囦竴榪炰覆鐨勬祴璇曞強楠岃瘉錛岃璁′竴緋誨垪鐨勫搧璐ㄦ帶鍒舵帰閽堬紝 浠ョ洃鎺у畬鏁寸殑鑺墖瀹為獙姝ラ錛屽寘鍚牱鏈?RNA 瀹屾暣鎬с€佹牱鏈?RNA 鏀懼ぇ嫻佺▼銆佽悿鍏夋爣璁版晥鐜囥€佽姱鐗囨潅浜ゃ€佽姱鐗囨壂鎻忕瓑銆?/font>
 

浣跨敤YOA鏂囩尞 ( 4 )

 Journal of Integrative Plant Biology. 2014 Jan 14. doi: 10.1111/jipb.12169.
 Identification of a novel pathway involving a GATA transcription factor in yeast and possibly plant Zn uptake and homeostasis 
 Matthew J. Milner, Nicole S. Pence, Jiping Liu, Leon V.Kochian
  Abstract
To gain a better understanding of the regulation of Zn homeostasis in plants and the degree of conservation of Zn homeostasis between plants and yeast, a cDNA library from the Zn/Cd hyperaccumulating plant species, Noccaea caerulescens, was screened for its ability to restore growth under Zn limiting conditions in the yeast mutant zap1▵. ZAP1 is a transcription factor that activates the Zn dependent transcription of genes involved in Zn uptake, including ZRT1, the yeast high affinity Zn transporter. From this screen two members of the E2F family of transcription factors were found to activate ZRT1 expression in a Zn independent manner. The activation of ZRT1 by the plant E2F proteins involves E2F-mediated activation of a yeast GATA transcription factor which in turn activates ZRT1 expression. A ZRT1 promoter region necessary for activation by E2F and GATA proteins is upstream of two zinc responsive elements previously shown to bind ZAP1 in ZRT1. This activation may not involve direct binding of E2F to the ZRT1 promoter. The expression of E2F genes in yeast does not replace function of ZAP1; instead it appears to activate a novel GATA regulatory pathway involved in Zn uptake and homeostasis that is not Zn responsive.
   

 Journal of Agricultural and Food Chemistry. 2013 Jun 10. doi: 10.1021/jf401831e.
 Tangeretin sensitizes SGS1 deficient cells by inducing DNA damage
 
 
 Shin Yen Chong, Meng-Ying Wu, Yi-Chen Lo
  Abstract
Tangeretin, a polymethoxyflavone found in citrus peel, has been shown to have anti-atherogenic, anti-inflammatory, and anti-carcinogenic properties. However, the underlying target pathways are not fully characterized. We investigated the tangeretin sensitivity of yeast (Saccharomyces cerevisiae) mutants for DNA damage response or repair pathways. We found that tangeretin treatment significantly reduced (p < 0.05) survival rate, induced preferential G1 phase accumulation, and elevated the DNA double-strand break (DSB) signal 緯H2A in DNA repair-defective sgs1螖 cells, but had no obvious effects on wild-type cells or mutants of the DNA damage checkpoint (including tel1∆, sml1∆ mec1∆, sml1∆ mec1∆ tel1∆, and rad9∆ mutants). Additionally, microarray data indicated that tangeretin treatment up-regulates genes involved in nutritional processing and down-regulates genes related to RNA processing in sgs1∆ mutants. These results suggest tangeretin may sensitize SGS1 deficient cells by increasing a marker of DNA damage, and by inducing G1 arrest and possibly metabolic stress. Thus, tangeretin may be suitable for chemosensitization of cancer cells lacking DSB-repair ability.
   

 Metabolic Engineering. 2012, 14(6):611-22. doi: 10.1016/j.ymben.2012.07.011.
 Xylose isomerase overexpression along with engineering of the pentose phosphate pathway and evolutionary engineering enable rapid xylose utilization and ethanol production by Saccharomyces cerevisiae
 
 
 Hang Zhou, Jing-sheng Cheng, Benjamin Wang, Gerald R. Fink, Gregory Stephanopoulos
  Abstract
Xylose is the main pentose and second most abundant sugar in lignocellulosic feedstocks. To improve xylose utilization, necessary for the cost-effective bioconversion of lignocellulose, several metabolic engineering approaches have been employed in the yeast Saccharomyces cerevisiae. In this study, we describe the rational metabolic engineering of a S. cerevisiae strain, including overexpression of the Piromyces xylose isomerase gene (XYLA), Pichia stipitis xylulose kinase (XYL3) and genes of the non-oxidative pentose phosphate pathway (PPP). This engineered strain (H131-A3) was used to initialize a three-stage process of evolutionary engineering, through first aerobic and anaerobic sequential batch cultivation followed by growth in a xylose-limited chemostat. The evolved strain H131-A3-ALCS displayed significantly increased anaerobic growth rate (0.203鹵0.006 h?1) and xylose consumption rate (1.866 g g?1 h?1) along with high ethanol conversion yield (0.41 g/g). These figures exceed by a significant margin any other performance metrics on xylose utilization and ethanol production by S. cerevisiae reported to-date. Further inverse metabolic engineering based on functional complementation suggested that efficient xylose assimilation is attributed, in part, to the elevated expression level of xylose isomerase, which was accomplished through the multiple-copy integration of XYLA in the chromosome of the evolved strain.
   

 PLoS One.. 2011, 6(7):e22209. doi: 10.1371/journal.pone.0022209.
 The C-Terminus of Histone H2B Is Involved in Chromatin Compaction Specifically at Telomeres, Independently of Its Monoubiquitylation at Lysine 123
 
 
 Wang CY, Hua CY, Hsu HE, Hsu CL, Tseng HY, Wright DE, Hsu PH, Jen CH, Lin CY, Wu MY, Tsai MD, Kao CF.
  Abstract
Telomeric heterochromatin assembly in budding yeast propagates through the association of Silent Information Regulator (SIR) proteins with nucleosomes, and the nucleosome array has been assumed to fold into a compacted structure. It is believed that the level of compaction and gene repression within heterochromatic regions can be modulated by histone modifications, such as acetylation of H3 lysine 56 and H4 lysine 16, and monoubiquitylation of H2B lysine 123. However, it remains unclear as to whether or not gene silencing is a direct consequence of the compaction of chromatin. Here, by investigating the role of the carboxy-terminus of histone H2B in heterochromatin formation, we identify that the disorderly compaction of chromatin induced by a mutation at H2B T122 specifically hinders telomeric heterochromatin formation. H2B T122 is positioned within the highly conserved AVTKY motif of the 偽C helix of H2B. Heterochromatin containing the T122E substitution in H2B remains inaccessible to ectopic dam methylase with dramatically increased mobility in sucrose gradients, indicating a compacted chromatin structure. Genetic studies indicate that this unique phenotype is independent of H2B K123 ubiquitylation and Sir4. In addition, using ChIP analysis, we demonstrate that telomere structure in the mutant is further disrupted by a defect in Sir2/Sir3 binding and the resulting invasion of euchromatic histone marks. Thus, we have revealed that the compaction of chromatin per se is not sufficient for heterochromatin formation. Instead, these results suggest that an appropriately arrayed chromatin mediated by H2B C-terminus is required for SIR binding and the subsequent formation of telomeric chromatin in yeast, thereby identifying an intrinsic property of the nucleosome that is required for the establishment of telomeric heterochromatin. This requirement is also likely to exist in higher eukaryotes, as the AVTKY motif of H2B is evolutionarily conserved.
   

五星单式稳赚
锘?div id="footer">

鐗堟潈澹版槑 | ©2006 - 2016 Copyright Phalanx Biotech All rights reserved.
鍗庤仈鐢熺墿縐戞妧鑲′喚鏈夐檺鍏徃        30078 鏂扮甯傜瀛﹀伐涓氬洯鍖虹鎶€浜旇礬6鍙?妤?nbsp;       E-mail : [email protected]


锘?
Pathway Map