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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The location of the structural gene for aggregation substance on the sex pheromone plasmid pAD1 of Enterococcus faecalis was determined using an oligonucleotide deduced from the N-terminal amino acid sequence of the purified protein. The nucleotide sequence was determined for the corresponding region and two open reading frames (ORFs) could be identified. ORF1 codes for a small (Mr 13,160) acidic protein of unknown function. The gene for aggregation substance (named asa1) was found to code for a protein of 1296 amino acids (Mr 142,248). The protein has a signal peptide of 43 amino acids (the resulting Mr for mature aggregation substance is 137,429) and contains in its C-terminal region a proline-rich sequence, previously characterized as being involved in cell wall association, which is followed by a membrane anchor. The membrane anchor showed significant similarity to that of other Gram-positive organisms, but no other similarities to surface proteins from Gram-positive bacteria were found. In particular, no repeats on the DNA or protein level could be detected for pAD1-specific aggregation substance. The protein contains the amino acid motifs Arg-Gly-Asp-Ser and Arg-Gly-Asp-Val (once each), which, it is proposed, play a crucial role in adherence to eukaryotic cells.
Mol Microbiol 1990 Jun
PMID:Sequence analysis of Enterococcus faecalis aggregation substance encoded by the sex pheromone plasmid pAD1. 212 May 41

Asexual development in Neurospora crassa proceeds through a series of discrete morphological stages that culminate in the production of dormant spores called conidia. Changes in the pattern of gene expression parallel the morphological transformations associated with conidiation. As a prerequisite to the analysis of developmental gene expression in N. crassa, several genes of unknown function that are preferentially expressed during conidiation were isolated [Berlin and Yanofsky, Mol. Cell. Biol. 5 (1985) 849-855]. The molecular structure and nucleotide sequence of one of these genes, designated con-13, is presented. The con-13 gene specifies a relatively rare 1.35-kb message which is first detected about 8 h following the induction of conidiation. Sequence analysis of both cDNA and genomic clones indicates that the con-13 gene consists of three exons divided by two small introns. It encodes a polypeptide of 340 amino acid residues (37.1 kDa). The Con-13 protein is weakly acidic and hydrophilic. A comparison of the regions upstream from the con-8, con-10, and con-13 genes revealed several short sequence motifs which may be important in developmental gene regulation.
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PMID:Genes expressed during conidiation in Neurospora crassa: molecular characterization of con-13. 214 38

Ammonium sulfate fractionation of a Saccharomyces cerevisiae whole-cell extract yielded a preparation which carried out correct and efficient endonucleolytic cleavage and polyadenylation of yeast precursor mRNA substrates corresponding to a variety of yeast genes. These included CYC1 (iso-1-cytochrome c), HIS4 (histidine biosynthesis), GAL7 (galactose-1-phosphate uridyltransferase), H2B2 (histone H2B2), PRT2 (a protein of unknown function), and CBP1 (cytochrome b mRNA processing). The reaction processed these pre-mRNAs with varying efficiencies, with cleavage and polyadenylation exceeding 70% in some cases. In each case, the poly(A) tail corresponded to the addition of approximately 60 adenosine residues, which agrees with the usual length of poly(A) tails formed in vivo. Addition of cordycepin triphosphate or substitution of CTP for ATP in these reactions inhibited polyadenylation but not endonucleolytic cleavage and resulted in accumulation of the cleaved RNA product. Although this system readily generated yeast mRNA 3' ends, no processing occurred on a human alpha-globin pre-mRNA containing the highly conserved AAUAAA polyadenylation signal of higher eucaryotes. This sequence and adjacent signals used in mammalian systems are thus not sufficient to direct mRNA 3' end formation in yeast. Despite the lack of a highly conserved nucleotide sequence signal, the same purified fraction processed the 3' ends of a variety of unrelated yeast pre-mRNAs, suggesting that endonuclease cleavage and polyadenylation may produce the mature 3' ends of all mRNAs in S. cerevisiae.
Mol Cell Biol 1990 Jun
PMID:RNA processing in vitro produces mature 3' ends of a variety of Saccharomyces cerevisiae mRNAs. 216 May 81

We have studied the organization of the expression site, in which most chromosome-internal variant-specific surface glycoprotein (VSG) genes of Trypanosoma brucei strain 427 are expressed (the dominant expression site) and compared it to the previously characterized VSG 221 expression site. With the exception of a 500 bp segment and a VSG pseudogene, which are absent from the dominant expression site, overall all major sequence elements of the two sites are organized similarly, as judged from their relative mapping positions by UV inactivation of transcription. Transcription is insensitive to 1 mg alpha-amanitin per ml, a characteristic property of VSG gene expression sites analyzed thus far. The sequence elements of the dominant expression site include at least one other expressed gene of unknown function and homologues of at least two other open reading frames. The large internal duplication of the 60-kb 221 expression site appear to be missing from the dominant site, resulting in a shorter, 40-kb transcription unit. As judged from its relative sensitivity to UV inactivation of transcription, a subsidiary promoter, identified by other methods in the dominant expression site appears fully dependent for its activity on the promoter located 40 kb upstream of the VSG gene. We conclude that all VSG gene expression sites may be similarly organized as large polygenic transcription units.
Mol Biochem Parasitol 1990 Aug
PMID:Structure of a telomeric expression site for variant specific surface antigens in Trypanosoma brucei. 223 94

The DNA sequence and transcriptional organization around the Escherichia coli methionyl-tRNA synthetase gene, metG, were resolved. This gene can be transcribed in vivo and in vitro from two distinct promoters separated by 510 nucleotides. The upstream promoter is located within the coding sequence of a divergent gene expressing a protein of Mr 39 kDa of unknown function. Transcription originating from this upstream promoter is attenuated by a Rho-independent terminator before entering the structural gene. This leader RNA contains several potentially stable secondary structures, one of which shows striking similarity to tRNA(Met), but no methionine-rich coding sequence. The regulation of metG expression was investigated by means of fusions to the lacZ gene. Transcription of a metG::lacZ fusion is induced in a metG mutant and, reciprocally, repression is observed in a methionyl-tRNA synthetase overproducing strain. A model of metG expression control is proposed.
Mol Gen Genet 1990 Aug
PMID:Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene. 225 34

Oligo(dA-dT) tracts are frequently found in the intergenic regions of the yeast Saccharomyces cerevisiae and have been proposed to act as upstream promoter elements for constitutive transcription. An oligo(dA-dT) tract of 23 bp is also found as a characteristic sequence motif in the centre of the 230 bp segment which separates the open reading frames of the CBS2 gene and its 5'-flanking gene on chromosome IV. Recently we have reported that transcription of CBS2 is initiated immediately adjacent to this oligo(dA-dT) tract (michaelis et al. 1988). Here we report that the flanking gene of unknown function is divergently transcribed into an RNA with heterogeneous 5' ends. Two of these 5' ends map within the oligo(dA-dT) stretch, while the third is located upstream, leading to an RNA species which is partially complementary to the CBS2 transcript. Gel shift assays show that the oligo(dA-dT) stretch is specifically recognized by (a) binding factor(s) in nuclear extracts. We discuss these results with respect to the role of oligo(dA-dT) stretches in gene expression in yeast.
Mol Gen Genet 1990 Sep
PMID:Transcription of two divergently transcribed yeast genes initiates at a common oligo(dA-dT) tract. 227 84

The pyrF gene, encoding the sixth enzyme of pyrimidine biosynthesis in Salmonella typhirmurium, appears to be the first gene of an operon. The second gene, orfF, encodes a 11.5 kDa polypeptide of unknown function. To study the regulation of orfF expression directly, transcriptional and translational fusions of orfF to galK and lacZ, respectively, were constructed and the level of expression of the reporter genes was determined under different growth conditions. The results obtained show that the synthesis of OrfF and orotidine 5'-phosphate decarboxylase is coordinately controlled by pyrimidines, and that this control occurs at the level of transcription. The orfF translational start codon overlaps the pyrF translational stop codon, suggesting that the two genes are translationally coupled. This was investigated by studying how frameshift mutations, which cause premature termination of pyrF translation at different points, affect orfF expression. All mutations reduced orfF expression markedly without interfering with transcription of the gene. Thus, expression of pyrF and orfF are translationally coupled. Inspection of the nucleotide sequence of the pyrF/orfF junction region suggests that formation of secondary structures on the naked mRNA may explain the low level of orfF expression in the absence of translation of the pyrF terminal region.
Mol Gen Genet 1990 Jul
PMID:Translational coupling in the pyrF operon of Salmonella typhimurium. 227 35

We have searched for induced transcripts in a cDNA library derived from bean cell supension cultures treated with an elicitor from Colletotrichum lindemuthianum. Six independently isolated cDNAs corresponding to rapidly induced small mRNAs have been classified by their DNA sequence and slightly different induction behaviour into two groups. 5'- and 3'-untranslated regions exhibit little similarity, but the deduced small acidic proteins designated PvPR1 and PvPR2 are 89% identical. No relationship was found with the well-characterized PR1 proteins from tobacco. However, the PvPR proteins are closely related to pI49 in pea (64% identity), pSTH2 in potato (41% identity) and PcPR1-1 in parsley (39% identity), which are also induced in response to elicitor or microbial attack. Moreover, a major pollen allergen in birch (BetvI) has a 44% identity with PvPR1 proteins. These similarities establish a ubiquitous class of conserved defense-related proteins and suggest a common yet still unknown function. Southern blot analysis indicates that PvPR protein gene organization is highly complex with an estimated copy number of more than 12 genes.
Mol Gen Genet 1990 Jul
PMID:Bean pathogenesis-related (PR) proteins deduced from elicitor-induced transcripts are members of a ubiquitous new class of conserved PR proteins including pollen allergens. 227 36

Cloned segments of the mouse glycerol-3-phosphate dehydrogenase (GPDH) gene, Gdc-1, were used to screen a human library. Human clones obtained spanned 25 kilobases of genomic DNA containing the human GPDH gene, GPD1. The 4 kb of sequence obtained from the 5'-flanking region and first exon of GPD1 was compared with the corresponding mouse sequence. Both sequences share a HindIII site located in what has proven to be the highly conserved 3' untranslated region of an upstream gene of unknown function, D15Kzl. The 3.6-kilobase segment of mouse DNA located between D15Kzl and Gdc-1 was provisionally termed the GPDH promoter. Alignment of the mouse promoter with the corresponding human sequence revealed two conserved domains. An upstream distal promoter region is approximately 900 base pairs in length. A downstream or proximal promoter region consists of approximately 300 base pairs immediately upstream of a TATA-like box and contains the fat-specific elements 1 and 2. Analysis of the chromatin structure of the Gdc-1 promoter revealed four DNase I-hypersensitive sites. They were present in DNA of liver and brown fat, in which GPDH expression is high, but were absent in DNA of spleen, in which GPDH expression is low. Methylation studies of the promoter showed it to be heavily methylated in sperm. However, the DNA from each adult somatic tissue had a unique distribution of nonmethylated sites and could easily be identified by its methylation pattern. These data suggest a structural model of the promoter that explains how Gdc-1 expression is differentially regulated in many types of cells.
Mol Cell Biol 1990 Oct
PMID:Sequence conservation and structural organization of the glycerol-3-phosphate dehydrogenase promoter in mice and humans. 239 90

ABFI (ARS-binding protein I) is a yeast protein that binds specific DNA sequences associated with several autonomously replicating sequences (ARSs). ABFI also binds sequences located in promoter regions of some yeast genes, including DED1, an essential gene of unknown function that is transcribed constitutively at a high level. ABFI was purified by specific binding to the DED1 upstream activating sequence (UAS) and was found to recognize related sequences at several other promoters, at an ARS (ARS1), and at a transcriptional silencer (HMR E). All ABFI-binding sites, regardless of origin, provided weak UAS function in vivo when examined in test plasmids. UAS function was abolished by point mutations that reduced ABFI binding in vitro. Analysis of the DED1 promoter showed that two ABFI-binding sites combine synergistically with an adjacent T-rich sequence to form a strong constitutive activator. The DED1 T-rich element acted synergistically with all other ABFI-binding sites and with binding sites for other multifunctional yeast activators. An examination of the properties of sequences surrounding ARS1 left open the possibility that ABFI enhances the initiation of DNA replication at ARS1 by transcriptional activation.
Mol Cell Biol 1990 Mar
PMID:A yeast ARS-binding protein activates transcription synergistically in combination with other weak activating factors. 240 70


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