Cotranscription of the genes encoding two P700 chlorophyll a apoproteins with the gene for ribosomal protein CS14: determination of the transcriptional initiation site by in vitro capping

1988 ◽  
Vol 14 (4) ◽  
pp. 395-400 ◽  
Author(s):  
Bing Yuan Meng ◽  
Minoru Tanaka ◽  
Tatsuya Wakasugi ◽  
Masaru Ohme ◽  
Kazuo Shinozaki ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Chlorophyll A ◽  
Initiation Site ◽  
Transcriptional Initiation ◽  
Genes Encoding ◽  
In Vitro Capping ◽  
Transcriptional Initiation Site

scholarly journals Genes encoding components of the olfactory signal transduction cascade contain a DNA binding site that may direct neuronal expression.

1993 ◽  
Vol 13 (9) ◽  
pp. 5805-5813 ◽  
Author(s):  
M M Wang ◽  
R Y Tsai ◽  
K A Schrader ◽  
R R Reed
Keyword(s):  
Signal Transduction ◽  
Dna Binding ◽  
Binding Site ◽  
Binding Sites ◽  
Consensus Sequence ◽  
Initiation Site ◽  
Olfactory Neuron ◽  
Promoter Regions ◽  
Transcriptional Initiation ◽  
Genes Encoding

Genes which mediate odorant signal transduction are expressed at high levels in neurons of the olfactory epithelium. The molecular mechanism governing the restricted expression of these genes likely involves tissue-specific DNA binding proteins which coordinately activate transcription through sequence-specific interactions with olfactory promoter regions. We have identified binding sites for the olfactory neuron-specific transcription factor, Olf-1, in the sequences surrounding the transcriptional initiation site of five olfactory neuron-specific genes. The Olf-1 binding sites described define the consensus sequence YTCCCYRGGGAR. In addition, we have identified a second binding site, the U site, in the olfactory cyclic nucleotide gated channel and type III cyclase promoters, which binds factors present in all tissue examined. These experiments support a model in which expression of Olf-1 in the sensory neurons coordinately activates a set of olfactory neuron-specific genes. Furthermore, expression of a subset of these genes may be modulated by additional binding factors.

scholarly journals Involvement of the C-Terminal Extension of the α Polypeptide and of the PucC Protein in LH2 Complex Biosynthesis in Rubrivivax gelatinosus

2004 ◽  
Vol 186 (10) ◽  
pp. 3143-3152 ◽  
Author(s):  
Anne-Soisig Steunou ◽  
Soufian Ouchane ◽  
Françoise Reiss-Husson ◽  
Chantal Astier
Keyword(s):  
Purple Bacteria ◽  
Growth Conditions ◽  
Initiation Site ◽  
Northern Blotting ◽  
Pcr Analysis ◽  
Reverse Transcription Pcr ◽  
Genes Encoding ◽  
Rubrivivax Gelatinosus

ABSTRACT The facultative phototrophic nonsulfur bacterium Rubrivivax gelatinosus exhibits several differences from other species of purple bacteria in the organization of its photosynthetic genes. In particular, the puc operon contains only the pucB and pucA genes encoding the β and α polypeptides of the light-harvesting 2 (LH2) complex. Downstream of the pucBA operon is the pucC gene in the opposite transcriptional orientation. The transcription of pucBA and pucC has been studied. No pucC transcript was detected either by Northern blotting or by reverse transcription-PCR analysis. The initiation site of pucBA transcription was determined by primer extension, and Northern blot analysis revealed the presence of two transcripts of 0.8 and 0.65 kb. The half-lives of both transcripts are longer in cells grown semiaerobically than in photosynthetically grown cells, and the small transcript is the less stable. It was reported that the α polypeptide, encoded by the pucA gene, presents a C-terminal extension which is not essential for LH2 function in vitro. The biological role of this alanine- and proline-rich C-terminal extension in vivo has been investigated. Two mutants with C-terminal deletions of 13 and 18 residues have been constructed. Both present the two pucBA transcripts, while their phenotypes are, respectively, LH2+ and LH2−, suggesting that a minimal length of the C-terminal extension is required for LH2 biogenesis. Another important factor involved in the LH2 biogenesis is the PucC protein. To gain insight into the function of this protein in R. gelatinosus, we constructed and characterized a PucC mutant. The mutant is devoid of LH2 complex under semiaerobiosis but still produces a small amount of these antennae under photosynthetic growth conditions. This conditional phenotype suggests the involvement of another factor in LH2 biogenesis.

Characterization of the human intestinal CD98 promoter and its regulation by interferon-γ

2007 ◽  
Vol 292 (2) ◽  
pp. G535-G545 ◽  
Author(s):  
Yutao Yan ◽  
Guillaume Dalmasso ◽  
Shanthi Sitaraman ◽  
Didier Merlin
Keyword(s):  
Transcriptional Regulation ◽  
Intestinal Inflammation ◽  
Direct Sequencing ◽  
Interferon Γ ◽  
Initiation Site ◽  
Start Codon ◽  
Transcriptional Initiation ◽  
Ifn Γ

Growing evidence that epithelial CD98 plays an important role in intestinal inflammation focused our interest to investigate the transcriptional regulation of CD98. Our mouse-based in vivo and in vitro experiments revealed that epithelial colonic CD98 mRNA expression was transcriptionally increased in intestinal inflammation. We then isolated and characterized a 5′-flanking fragment containing the promoter region required for CD98 gene transcription. Primer extension and rapid amplification of 5′-cDNA ends were used to map a transcriptional initiation site 129 bp upstream from the translational start codon (ATG). Direct sequencing of the 5′-flanking region revealed the presence of four GC-rich stimulating protein (Sp)1 binding domains, one NF-κB binding domain, and no TATA box. Binding of Sp1 [Sp1(−874), SP1(−386), Sp1(−187), and Sp1(−177)] and NF-κB [NF-κB(−213)] to the promoter was confirmed by EMSA and supershift assays. Furthermore, chromatin immunoprecipitation experiments showed the in vivo DNA-Sp1 and DNA-NF-κB interactions under basal and IFN-γ-stimulated conditions. Reporter genes driven by serially truncated and site-mutated CD98 promoters were used to examine basal and IFN-γ-responsive transcription in transiently transfected Caco2-BBE cells. Our results revealed that Sp1(−187), Sp1(−177), and the NF-κB binding site were essential for basal and IFN-γ-stimulated CD98 promoter activities, whereas Sp1(−874) and Sp1(−386) were not. The results from additional site-mutated CD98 promoters suggested that Sp1(−187), Sp1(−177), and the NF-κB site may cooperate in mediating basal and IFN-γ-stimulated CD98 promoter activities. Finally, we demonstrated that a reduction of Sp1 or NF-κB expression reduced CD98 protein expression in unstimulated and IFN-γ-stimulated Caco2-BBE cells. Collectively, these findings indicate that the Sp1 and NF-κB transcription factors are likely to play a significant role in IFN-γ-mediated transcriptional regulation of CD98 in the intestinal epithelium, providing new insights into the regulation of CD98 expression in intestinal inflammation.

scholarly journals Transcriptional initiation is controlled by upstream GC-box interactions in a TATAA-less promoter.

1990 ◽  
Vol 10 (12) ◽  
pp. 6632-6641 ◽  
Author(s):  
M C Blake ◽  
R C Jambou ◽  
A G Swick ◽  
J W Kahn ◽  
J C Azizkhan
Keyword(s):  
Dihydrofolate Reductase ◽  
Gene Promoter ◽  
In Vitro Transcription ◽  
Initiation Site ◽  
Start Site ◽  
Transcriptional Initiation ◽  
Reductase Gene ◽  
Gc Box

Numerous genes contain TATAA-less promoters, and the control of transcriptional initiation in this important promoter class is not understood. We have determined that protein-DNA interactions at three of the four proximal GC box sequence elements in one such promoter, that of the hamster dihydrofolate reductase gene, control initiation and relative use of the major and minor start sites. Our results indicate that although the GC boxes are apparently equivalent with respect to factor binding, they are not equivalent with respect to function. At least two properly positioned GC boxes were required for initiation of transcription. Abolishment of DNA-protein interaction by site-specific mutation of the most proximal GC box (box I) resulted in a fivefold decrease in transcription from the major initiation site and a threefold increase in heterogeneous transcripts initiating from the vicinity of the minor start site in vitro and in vivo. Mutations that separately abolished interactions at GC boxes II and III while leaving GC box I intact affected the relative utilization of both the major and minor initiation sites as well as transcriptional efficiency of the promoter template in in vitro transcription and transient expression assays. Interaction at GC box IV when the three proximal boxes were in a wild-type configuration had no effect on transcription of the dihydrofolate reductase gene promoter. Thus, GC box interactions not only are required for efficient transcription but also regulate start site utilization in this TATAA-less promoter.

A cloned human CCAAT-box-binding factor stimulates transcription from the human hsp70 promoter

1990 ◽  
Vol 10 (12) ◽  
pp. 6709-6717
Author(s):  
L S Lum ◽  
L A Sultzman ◽  
R J Kaufman ◽  
D I Linzer ◽  
B J Wu
Keyword(s):  
Initiation Site ◽  
Dependent Manner ◽  
Hsp70 Gene ◽  
Hsp70 Promoter ◽  
Transcriptional Initiation ◽  
Enhancer Binding Protein ◽  
Binding Factor ◽  
Ccaat Box ◽  
Transcriptional Initiation Site ◽  
Human Hsp70

The basal promoter of the human hsp70 gene is predominantly controlled by a CCAAT element at position -70 relative to the transcriptional initiation site. We report the isolation of a novel cDNA clone encoding a 114-kDa polypeptide that binds to the CCAAT element of the hsp70 promoter. Expression of this CCAAT-binding factor (CBF) cDNA activated transcription from cotransfected hsp70 promoter-reporter gene constructs in a CCAAT-dependent manner. CCAAT-binding factor shows no homology to the previously identified human CCAAT transcription factor or rat CCAAT/enhancer-binding protein.

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