scholarly journals Molecular and Genetic Characterization of a Taf1p Domain Essential for Yeast TFIID Assembly

2004 ◽  
Vol 24 (11) ◽  
pp. 4929-4942 ◽  
Author(s):  
Madhu V. Singh ◽  
Christin E. Bland ◽  
P. Anthony Weil
Keyword(s):  
Genetic Characterization ◽  
Yeast Cells ◽  
Deletion Mutants ◽  
Mrna Synthesis ◽  
Reading Frame ◽  
Entire Open Reading Frame ◽  
And Function ◽  
Tfiid Complex

ABSTRACT Yeast Taf1p is an integral component of the multiprotein transcription factor TFIID. By using coimmunoprecipitation assays, coupled with a comprehensive set of deletion mutants encompassing the entire open reading frame of TAF1, we have discovered an essential role of a small portion of yeast Taf1p. This domain of Taf1p, termed region 4, consisting of amino acids 200 to 303, contributes critically to the assembly and stability of the 15-subunit TFIID holocomplex. Region 4 of Taf1p is mutationally sensitive, can assemble several Tafps into a partial TFIID complex, and interacts directly with Taf4p and Taf6p. Mutations in Taf1p-region 4 induce temperature-conditional growth of yeast cells. At the nonpermissive temperature these mutations have drastic effects on both TFIID integrity and mRNA synthesis. These data are consistent with the hypothesis that Taf1p subserves a critical scaffold function within the TFIID complex. The significance of these data with regard to TFIID structure and function is discussed.

Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit

1993 ◽  
Vol 13 (12) ◽  
pp. 7859-7863
Author(s):  
T Kokubo ◽  
D W Gong ◽  
S Yamashita ◽  
R Takada ◽  
R G Roeder ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
Initiation Factor ◽  
Transcriptional Regulatory ◽  
Transcription Initiation Factor ◽  
Multimeric Protein ◽  
And Function ◽  
Tfiid Complex ◽  
Binding Subunit

Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. To further understand the role of the 85-kDa TFIID subunit (p85), we have cloned the corresponding cDNA with a probe based on an amino acid sequence of the purified protein. The recombinant p85 interacts directly with both the TATA box-binding subunit (TFIID tau or TBP) and the 110-kDa subunit (p110) of TFIID, suggesting that p85 may play a role in helping to anchor p110 within the TFIID complex and, with other studies, that TFIID assembly and function may involve a concerted series of subunit interactions. Interestingly, the carboxy terminus of p85 contains eight of the WD-40 repeats found originally in the beta subunit of G proteins and more recently in other transcriptional regulatory factors. However, truncated p85 lacking all the WD-40 repeats maintained interactions with both TFIID tau and p110. These observations leave open the possibility of a distinct function for the WD-40 repeats, possibly in transducing signals by interactions with transcriptional regulators and/or other components of the basic transcriptional machinery.

scholarly journals Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit.

1993 ◽  
Vol 13 (12) ◽  
pp. 7859-7863 ◽  
Author(s):  
T Kokubo ◽  
D W Gong ◽  
S Yamashita ◽  
R Takada ◽  
R G Roeder ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
Initiation Factor ◽  
Transcriptional Regulatory ◽  
Transcription Initiation Factor ◽  
Multimeric Protein ◽  
And Function ◽  
Tfiid Complex ◽  
Binding Subunit

Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. To further understand the role of the 85-kDa TFIID subunit (p85), we have cloned the corresponding cDNA with a probe based on an amino acid sequence of the purified protein. The recombinant p85 interacts directly with both the TATA box-binding subunit (TFIID tau or TBP) and the 110-kDa subunit (p110) of TFIID, suggesting that p85 may play a role in helping to anchor p110 within the TFIID complex and, with other studies, that TFIID assembly and function may involve a concerted series of subunit interactions. Interestingly, the carboxy terminus of p85 contains eight of the WD-40 repeats found originally in the beta subunit of G proteins and more recently in other transcriptional regulatory factors. However, truncated p85 lacking all the WD-40 repeats maintained interactions with both TFIID tau and p110. These observations leave open the possibility of a distinct function for the WD-40 repeats, possibly in transducing signals by interactions with transcriptional regulators and/or other components of the basic transcriptional machinery.

Characterization of anEscherichia coliSulfite Oxidase Homologue Reveals the Role of a Conserved Active Site Cysteine in Assembly and Function†

Biochemistry ◽  
2005 ◽  
Vol 44 (30) ◽  
pp. 10339-10348 ◽  
Author(s):  
Stephen J. Brokx ◽  
Richard A. Rothery ◽  
Guijin Zhang ◽  
Derek P. Ng ◽  
Joel H. Weiner
Keyword(s):  
Active Site ◽  
Active Site Cysteine ◽  
And Function

scholarly journals Identification and Characterization of the PutP Proline Permease That Contributes to In Vivo Survival ofStaphylococcus aureus in Animal Models

1998 ◽  
Vol 66 (2) ◽  
pp. 567-572 ◽  
Author(s):  
William R. Schwan ◽  
Silvija N. Coulter ◽  
Eva Y. W. Ng ◽  
Michael H. Langhorne ◽  
Heather D. Ritchie ◽  
...  
Keyword(s):  
Animal Models ◽  
Reading Frame ◽  
High Affinity ◽  
Wound Model ◽  
Infection Models ◽  
Uptake Assay ◽  
Entire Open Reading Frame ◽  
In Vivo Growth

ABSTRACT Staphylococcus aureus is an important pathogen of humans and other animals, causing bacteremia, abscesses, endocarditis, and other infectious syndromes. A signature-tagged mutagenesis (STM) system was adapted for use in studying the genes required for in vivo survival of S. aureus. An STM library was ultimately created in S. aureus RN6390, with Tn917 being used to create the transposon mutations. Pools of S. aureusRN6390 mutants were screened in mouse abscess, bacteremia, and wound infection models for growth attenuation after in vivo passage. One of the mutants that was identified displayed marked attenuation following large-pool screening in all three animal models, which was confirmed in bacteremia and endocarditis models of infection with a smaller pool of mutants. Sequence analysis of the entire open reading frame showed a 99% identity to the high-affinity proline permease (putP) gene characterized in another strain of S. aureus. In wound and murine abscess infection models, the putP mutant was approximately 10-fold more attenuated than was wild-type strain RN6390. Another S. aureus strain transduced with theputP mutation also displayed an attenuated phenotype after passage in the wound model. A [3H]proline uptake assay showed that less proline was specifically transported into theputP mutant than into strain RN6390. The reduced viability of the bacteria possessing the mutation in the S. aureushigh-affinity proline permease suggests that proline scavenging by the bacteria is important for in vivo growth and proliferation and that analogs of proline may serve as potential antistaphylococcal therapeutic agents.

scholarly journals Characterization of hepatitis B virus genotypes among Yucpa Indians in Venezuela

2001 ◽  
Vol 82 (2) ◽  
pp. 359-365 ◽  
Author(s):  
Tatsunori Nakano ◽  
Ling Lu ◽  
Xiaolei Hu ◽  
Masashi Mizokami ◽  
Etsuro Orito ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Complete Genome ◽  
Deletion Mutants ◽  
Reading Frame ◽  
B Virus ◽  
Virus Genotypes ◽  
Core Reading ◽  
Genotype F

The complete genome sequences of hepatitis B virus (HBV) from 12 HBV-infected Yucpa Indians of Venezuela, a group with highly endemic HBV, were amplified and sequenced. The 12 isolates were closely related to each other, with 98·6–100% nucleotide identity. A phylogenetic tree based on the complete genome indicated clearly that they were genotype F. Three individuals had evidence of infection with two different HBV deletion mutants. In two individuals, a three amino acid deletion was identified just prior to the ‘a’ determinant loop of the S region. A third individual was infected with virus that contained a complete core reading frame and a population that contained a deletion in the middle of the core region. These results indicate that genotype F HBV is present in the Venezuelan Yucpa Amerindians and the complete genome sequence allowed the identification of two unique deletion mutants in a limited set of samples.

Biological and genetic characterization of the role of SRSF2 mutations in the pathogenesis of myelodysplastic syndromes

2015 ◽  
Vol 43 (9) ◽  
pp. S73
Author(s):  
Ayana Kon ◽  
Satoshi Yamazaki ◽  
Keisuke Kataoka ◽  
Tetsuichi Yoshizato ◽  
Yusuke Shiozawa ◽  
...  
Keyword(s):  
Myelodysplastic Syndromes ◽  
Genetic Characterization

scholarly journals Role of the INDETERMINATE DOMAIN Genes in Plants

2019 ◽  
Vol 20 (9) ◽  
pp. 2286 ◽  
Author(s):  
Manu Kumar ◽  
Dung Thi Le ◽  
Seongbin Hwang ◽  
Pil Joon Seo ◽  
Hyun Uk Kim
Keyword(s):  
Plant Architecture ◽  
Genetic Characterization ◽  
Sugar Metabolism ◽  
Hormone Signaling ◽  
Biological Functions ◽  
Transcription Factor Family ◽  
Physiological Processes ◽  
Ammonium Metabolism

The INDETERMINATE DOMAIN (IDD) genes comprise a conserved transcription factor family that regulates a variety of developmental and physiological processes in plants. Many recent studies have focused on the genetic characterization of IDD family members and revealed various biological functions, including modulation of sugar metabolism and floral transition, cold stress response, seed development, plant architecture, regulation of hormone signaling, and ammonium metabolism. In this review, we summarize the functions and working mechanisms of the IDD gene family in the regulatory network of metabolism and developmental processes.

scholarly journals Isolation and Characterization of Cryptococcus neoformans Spores Reveal a Critical Role for Capsule Biosynthesis Genes in Spore Biogenesis

2009 ◽  
Vol 8 (4) ◽  
pp. 595-605 ◽  
Author(s):  
Michael R. Botts ◽  
Steven S. Giles ◽  
Marcellene A. Gates ◽  
Thomas R. Kozel ◽  
Christina M. Hull
Keyword(s):  
Cryptococcus Neoformans ◽  
Fungal Pathogens ◽  
Critical Role ◽  
Spore Formation ◽  
Yeast Cells ◽  
Isolation And Characterization ◽  
Specific Configuration ◽  
First Time

ABSTRACT Spores are essential particles for the survival of many organisms, both prokaryotic and eukaryotic. Among the eukaryotes, fungi have developed spores with superior resistance and dispersal properties. For the human fungal pathogens, however, relatively little is known about the role that spores play in dispersal and infection. Here we present the purification and characterization of spores from the environmental fungus Cryptococcus neoformans. For the first time, we purified spores to homogeneity and assessed their morphological, stress resistance, and surface properties. We found that spores are morphologically distinct from yeast cells and are covered with a thick spore coat. Spores are also more resistant to environmental stresses than yeast cells and display a spore-specific configuration of polysaccharides on their surfaces. Surprisingly, we found that the surface of the spore reacts with antibodies to the polysaccharide glucuronoxylomannan, the most abundant component of the polysaccharide capsule required for C. neoformans virulence. We explored the role of capsule polysaccharide in spore development by assessing spore formation in a series of acapsular strains and determined that capsule biosynthesis genes are required for proper sexual development and normal spore formation. Our findings suggest that C. neoformans spores may have an adapted cell surface that facilitates persistence in harsh environments and ultimately allows them to infect mammalian hosts.

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