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PBF-2 is a novel single-stranded DNA binding factor implicated in PR-10a gene activation in potato

PLANT CELL 2000年第8期12卷 1477-1489页

作者： Desveaux, D Després, C Joyeux, A Subramaniam, R Brisson, N Univ Montreal Dept Biochem Montreal PQ H3C 3J7 Canada

Elicitor-induced activation of the potato pathogenesis-related gene PR-10a requires a 30-bp promoter sequence termed the ERE (elicitor response element) that is bound by the nuclear factor PBF-2 (PR-10a binding factor 2). In this study, PBF-2 has been purified to near homogeneity from elicited tubers through a combination of anion-exchange and DNA affinity chromatography. Evidence demonstrates that inactive PBF-2 is stored in the nuclei of fresh tubers and becomes available for binding to the ERE upon elicitation. A protein with an apparent molecular mass of 24 kD (p24) is a DNA binding component of PBF-2. A cDNA encoding p24 has been cloned and encodes a novel protein with a potential transcriptional activation domain that could also act as a single-stranded DNA binding domain. Both PBF-2 and the cDNA-encoded protein bind with high affinity to the single-stranded form of the ERE in a sequence-specific manner. The inverted repeat sequence of the ERE, TGACAnnnnTGTCA, is critical for binding of this factor in vitro and for PR-10a expression in vivo, supporting the role of PBF-2 as a transcriptional regulator.

关键词：氨基酸序列抗体/免疫学抗体/药理学碱基序列结合部位细胞核/化学细胞核/药物作用细胞核/代谢色谱法亲和克隆分子 DNA 单链/遗传学 DNA 单链/代谢 DNA结合蛋白质类/化学 DNA结合蛋白质类/遗传学 DNA结合蛋白质类/分离和提纯 DNA结合蛋白质类/代谢基因表达调控植物/药物作用基因植物/遗传学基因报告/遗传学模型遗传学分子序列数据分子量突变核蛋白质类/化学核蛋白质类/遗传学核蛋白质类/分离和提纯核蛋白质类/代谢肽类/化学肽类/遗传学植物生长调节物/药理学植物蛋白质类蛋白质结合/药物作用重组蛋白质类/化学重组蛋白质类/遗传学重组蛋白质类/分离和提纯重组蛋白质类/代谢反应元件/遗传学马铃薯/细胞学马铃薯/药物作用马铃薯/遗传学底物特异性反式激活因子类/化学反式激活因子类/遗传学反式激活因子类/分离和提纯反式激活因子类/代谢

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The α and β subunit of the nascent polypeptide-associated complex have distinct functions

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第48期275卷 37838-37845页

作者： Beatrix, B Sakai, H Wiedmann, M Mem Sloan Kettering Canc Ctr Cellular Biochem & Biophys Program New York NY 10021 USA Nagasaki Univ Sch Dent Dept Pharmacol Nagasaki 852 Japan

Nascent polypeptide-associated complex (NAC) is probably the first cytosolic protein to contact nascent polypeptide chains emerging from ribosomes. In this way NAC prevents inappropriate interactions with other factors. Eventually other factors involved in targeting and folding, like the Signal Recognition Particle or cytosolic chaperones, must gain access to the nascent chain. AU. NAC preparations to date consist of two copurifying polypeptides. Here we rigorously show that these two polypeptides, termed alpha- and beta NAC, form a very stable complex in vivo and in vitro and that a functional complex can be reconstituted from the individual subunits. A dissection of the contributions of the individual subunits to NACs function revealed that both subunits are in direct contact with nascent polypeptide chains on the ribosome and that both contribute to the prevention of inappropriate interactions. However, beta NAC alone directly binds to the ribosome and is sufficient to prevent ribosome binding to the endoplasmic reticulum membrane.

关键词：氨基酸序列细胞系色谱法凝胶免疫组织化学分子监控蛋白类分子序列数据核酸类/代谢重组蛋白质类/化学重组蛋白质类/分离和提纯重组蛋白质类/代谢信号识别颗粒/代谢反式激活因子类/化学反式激活因子类/分离和提纯反式激活因子类/代谢动物狗小鼠

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Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator

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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 2000年第11期97卷 6212-6217页

作者： Ko, L Cardona, GR Chin, WW Harvard Univ Brigham & Womens Hosp Sch Med Dept MedDiv Genet Boston MA 02115 USA

Nuclear hormone receptors activate gene transcription through ligand-dependent association with coactivators, Specific LXLL sequence motifs present in these cofactors are sufficient to mediate these ligand-induced interactions. A thyroid hormone receptor (TR)-binding protein (TRBP) was cloned by a Sos-Ras yeast two-hybrid system using TR beta 1-ligand binding domain as bait. TRBP contains 2063 amino acid residues, associates with TR through a LXLL motif, and is ubiquitously expressed in a variety of tissues and cells. TRBP strongly transactivates through TR beta 1 and estrogen receptor in a dose-related and ligand-dependent manner, and also exhibits coactivation through AP-1, CRE, and NF kappa B-response elements, similar to the general coactivator CBP/p300, The C terminus of TRBP binds to CBP/p300 and DRIP130, a component of the DRIP/TRAP/ARC complex, which suggests that TRBP may activate transcription by means of such interactions. Further, the association of TRBP with the DNA-dependent protein kinase (DNA-PK) complex and DNA-independent phosphorylation of TRBP C terminus by DNA-PK point to a potential connection between transcriptional control and chromatin architecture regulation.

关键词：氨基酸特征结构氨基酸序列 CREB结合蛋白质细胞系细胞核/代谢黑长尾猴 DNA活化蛋白激酶 DNA结合蛋白质类基因报告 HeLa细胞细胞内信号肽和蛋白质类中介体复合物分子序列数据核蛋白质类/代谢核受体共激活因子类蛋白质丝氨酸苏氨酸激酶/代谢受体雌激素/生理学受体甲状腺激素/生理学重组融合蛋白质类/代谢反式激活因子类/化学反式激活因子类/遗传学反式激活因子类/分离和提纯反式激活因子类/代谢反式激活因子类/生理学转录因子/代谢转录遗传转染双杂交系统技术动物人类

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Isolation and characterization of HsfA3, a new heat stress transcription factor of Lycopersicon peruvianum

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PLANT JOURNAL 2000年第4期22卷 355-365页

作者： Bharti, K Schmidt, E Lyck, R Heerklotz, D Bublak, D Scharf, KD Goethe Univ Frankfurt Bioctr N200 Dept Mol Cell Biol D-60439 Frankfurt Germany

Stress-induced transcription of heat shock proteins (Hsps) in eukaryotes is mediated by a conserved class of transcription factors called heat stress transcription factors (Hsfs). Here we report the isolation and functional characterization of HsfA3, a new member of the Hsf family. HsfA3 was cloned from a tomato heat stress cDNA library by yeast two-hybrid screening, using HsfA1 as a bait. HsfA3 is a single-copy gene with all the conserved sequence elements characteristic of a heat stress transcription factor. The constitutively expressed HsfA3 is mainly found in the cytoplasm under control conditions and in the nucleus under heat stress conditions. Functionally, HsfA3 behaves similarly to the already known members of tomato Hsf family. It is able to substitute yeast Hsf for viability functions and is a strong activator of Hsf-dependent reporter constructs both in tobacco protoplasts and yeast. Finally, similar to the AHA motifs in HsfA1 and HsfA2, the activator function depends on four short peptide motifs with a central tryptophan residue found in the C-terminal domain of HsfA3.

关键词：氨基酸序列碱基序列克隆分子 DNA引物 DNA 互补 DNA结合蛋白质类/化学 DNA结合蛋白质类/遗传学 DNA结合蛋白质类/分离和提纯热休克蛋白质类/化学热休克蛋白质类/遗传学热休克蛋白质类/分离和提纯番茄/细胞学番茄/代谢分子序列数据植物蛋白质类植物有毒原生质体/代谢烟草/代谢反式激活因子类/化学反式激活因子类/分离和提纯反式激活因子类/代谢转录因子/化学转录因子/遗传学转录因子/分离和提纯

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Poly(ADP-ribose) polymerase is a B-MYB coactivator

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第14期275卷 10692-10696页

作者： Cervellera, MN Sala, A Consorzio Mario Negri Sud Dept Mol Pharmacol & Pathol I-66030 Santa Maria Imbaro Chieti Italy

B-MYB is implicated in cell growth control, differentiation, and cancer and belongs to the MYB family of nuclear transcription factors. Evidence exists that cellular proteins bind directly to B-MYB, and it has been hypothesized that B-MYB transcriptional activity may be modulated by specific cofactors. In an attempt to isolate proteins that interact with the B-MYB DNA-binding domain, a modular domain that has the potential to mediate protein-protein interaction, we performed pull-down experiments with a glutathione S-transferase-B-MYB protein and mammalian protein extracts. We isolated a 110-kDa protein associated endogenously with B-MYB in the nuclei of HL60 cells. Microsequence analysis and immunoprecipitation experiments determined that the bound protein was poly(ADP-ribose) polymerase (PARP). Transient transfection assays showed that PARP enhanced B-MYB transactivation and that PARP enzymatic activity is not required for B-MYB-dependent transactivation. These results suggest that PARP, as a transcriptional cofactor of a potentially oncogenic protein, may play a role in growth control and cancer.

关键词：结合部位细胞周期蛋白质类细胞核/代谢 DNA结合蛋白质类/化学 DNA结合蛋白质类/分离和提纯 DNA结合蛋白质类/代谢谷胱甘肽转移酶 HL-60细胞哺乳动物癌基因蛋白质类/代谢骨肉瘤聚ADP核糖聚合酶类/遗传学聚ADP核糖聚合酶类/分离和提纯聚ADP核糖聚合酶类/代谢蛋白质生物合成重组融合蛋白质类/分离和提纯重组融合蛋白质类/代谢反式激活因子类/化学反式激活因子类/分离和提纯反式激活因子类/代谢转录遗传肿瘤细胞培养的动物人类

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MOZ is fused to p300 in an acute monocytic leukemia with t(8;22)

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GENES CHROMOSOMES & CANCER 2000年第2期28卷 138-144页

作者： Chaffanet, M Gressin, L Preudhomme, C Soenen-Cornu, V Birnbaum, D Pébusque, MJ INSERM U119 Oncol Mol Lab Inst Cancerol & Immunol Marseille F-13009 Marseille France Inst J Paoli I Calmettes Lab Biol Tumeurs F-13009 Marseille France Fdn Jean Dausset Paris France Hop Calmettes Hematol Lab Lille France

We report on the fusion of the monocytic leukemia zinc finger protein (MOZ) gene to the adenoviral EIA-associated protein p300 (p300) gene in acute monocytic leukemia M5 associated with a t(8;22)(p11;q13) translocation. We studied two patients with double-color fluorescence in situ hybridization (FISH) using the yeast artificial chromosome 176C9 and the bacterial artificial chromosome clone H59D10 specific to the MOZ and p300 genes, respectively. Both probes were split. in the patients' chromosome metaphase cells, and the two derivative chromosomes were each labeled with both probes. We showed by Southern blot the rearrangement of the MOZ gene, and cloned the fusion transcripts in one patient carrying the t(8;22) by reverse transcription-polymerase chain reaction using MOZ- and p300-specific primers. Both fusion transcripts were expressed. This result defines a novel reciprocal translocation involving Mo acetyltransferases, MOZ and p300, resulting in an: abnormal transcriptional co-activator that could play a critical role in leukemogenesis. Genes Chromosomes Cancer 28: 138-144, 2000. (C) 2000 Wiley-Liss, Inc.

关键词：乙酰基转移酶类/遗传学乙酰基转移酶类/分离和提纯氨基酸序列染色体人 22对/遗传学染色体人 8对/遗传学 E1A相关p300蛋白质基因重排组蛋白酰基转移酶原位杂交荧光白血病单核细胞急性/酶学白血病单核细胞急性/遗传学白血病粒-单核细胞慢性/酶学白血病粒-单核细胞慢性/遗传学分子序列数据核蛋白质类/遗传学核蛋白质类/分离和提纯 RNA 信使/分离和提纯重组融合蛋白质类/遗传学重组融合蛋白质类/分离和提纯反式激活因子类/遗传学反式激活因子类/分离和提纯易位遗传/遗传学肿瘤细胞培养的人类

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Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates

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MOLECULAR AND CELLULAR BIOLOGY 1999年第12期19卷 8123-8135页

作者： Kraus, WL Manning, ET Kadonaga, JT Univ Calif San Diego Dept Biol La Jolla CA 92093 USA Univ Calif San Diego Ctr Mol Genet La Jolla CA 92093 USA

To investigate the mechanisms of transcriptional enhancement by the p300 coactivator, we analyzed wildtype and mutant versions of p300 with a chromatin transcription system in vitro. Estrogen receptor, NF-kappa B p65 plus Sp1, and Gal4-VP16 were used as different sequence-specific activators. The CH3 domain (or E1A-binding region) was found to be essential for the function of each of the activators tested. The bromodomain was also observed to be generally important for p300 coactivator activity, though to a lesser extent than the CH3 domain/E1A-binding region. The acetyltransferase activity and the C-terminal region (containing the steroid receptor coactivator/p160-binding region and the glutamine-rich region) were each found to be important for activation by estrogen receptor but not for that by Gal4-VP16. The N-terminal region of p300, which had been previously found to interact with nuclear hormone receptors, was not seen to be required for any of the activators, including estrogen receptor. Single-round transcription experiments revealed that the functionally important subregions of p300 contribute to its ability to promote the assembly of transcription initiation complexes. In addition, the acetyltransferase activity of p300 was observed to be distinct from the broadly essential activation function of the CH3 domain/E1A-binding region. These results indicate that specific regions of p300 possess distinct activation functions that are differentially required to enhance the assembly of transcription initiation complexes. Interestingly, with the estrogen receptor, four distinct regions of p300 each have an essential role in the transcription activation process. These data exemplify a situation in which a network of multiple activation functions is required to achieve gene transcription.

关键词：乙酰基转移酶类/生物合成乙酰基转移酶类/分离和提纯乙酰基转移酶类/代谢腺病毒E1A蛋白质类/代谢氨基酸序列染色质 E1A相关p300蛋白质 HeLa细胞组蛋白酰基转移酶分子序列数据诱变核蛋白质类/生物合成核蛋白质类/分离和提纯核蛋白质类/代谢启动区遗传受体雌激素/代谢酿酒酵母蛋白质类模板遗传反式激活因子类/生物合成反式激活因子类/分离和提纯反式激活因子类/代谢转录遗传动物人类小鼠

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Purification of transcription cofactor complex CRSP

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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 1999年第13期96卷 7137-7142页

作者： Ryu, SJ Tjian, R Univ Calif Berkeley Howard Hughes Med Inst Berkeley CA 94720 USA

Transcription of protein coding genes in metazoans involves the concerted action of enhancer binding proteins and the RNA polymerase II apparatus. The cross talk between these two classes of transcription factors is mediated by an elaborate set of cofactor complexes, For the activation of transcription by the promoter specificity protein 1 (Spl), TATA binding protein-associated factors in the TFIID complex originally were identified as necessary coactivators, but the identity of additional cofactors required for activated transcription was unknown. Recently, we have reported the isolation and properties of a cofactor complex, CRSP (cofactor required for Sp1), which functions in conjunction with the TATA binding protein-associated factors to promote efficient activation of transcription by Sp1, CRSP contains unique subunits as well as polypeptides that are shared with other cofactor complexes, Here, we report a detailed purification protocol for the isolation of CRSP from human HeLa cells, Our purification strategy takes advantage of the ability of CRSP to bind Ni2+-nitrilotriacetic acid-agarose resin as well as other conventional chromatographic resins, We also describe a streamlined purification protocol that allows a more rapid and efficient means to isolate active CRSP.

关键词：色谱法亲和/方法 HeLa细胞大分子物质中介体复合物 Sp1转录因子/代谢反式激活因子类/遗传学反式激活因子类/分离和提纯反式激活因子类/代谢人类

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