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1.
FEBS Lett ; 445(2-3): 237-45, 1999 Feb 26.
Article in English | MEDLINE | ID: mdl-10094464

ABSTRACT

As part of the European Scientists Sequencing Arabidopsis program, a contiguous region (396607 bp) located on chromosome 4 around the APETALA2 gene was sequenced. Analysis of the sequence and comparison to public databases predicts 103 genes in this area, which represents a gene density of one gene per 3.85 kb. Almost half of the genes show no significant homology to known database entries. In addition, the first 45 kb of the contig, which covers 11 genes, is similar to a region on chromosome 2, as far as coding sequences are concerned. This observation indicates that ancient duplications of large pieces of DNA have occurred in Arabidopsis.


Subject(s)
Gene Duplication , Genes, Plant , Homeodomain Proteins/genetics , Nuclear Proteins/genetics , Plant Proteins/genetics , Arabidopsis/genetics , Arabidopsis Proteins , Base Sequence , Chromosome Mapping , Contig Mapping , DNA, Plant , Genome, Plant , Introns , Mathematical Computing , Molecular Sequence Data , Multigene Family
2.
Gene ; 215(1): 11-7, 1998 Jul 17.
Article in English | MEDLINE | ID: mdl-9666060

ABSTRACT

As a contribution to the European Scientists Sequencing Arabidopsis (BIOTECH ESSA) project, a contig of almost 40kb has been sequenced at the extreme top of chromosome 1, around the Arabidopsis thaliana gene coding for a member of the 1-aminocyclopropane-1-carboxylate synthesis gene family. The region contains, besides the ACS1 gene itself, 10 putative genes, all new for Arabidopsis. Among these are three genes encoding kinases, a late embryogenesis-abundant protein, a MADS box-containing protein, a dehydrogenase, and a Myb-related transcription factor. In addition, six cDNAs have been sequenced that correspond to this region.


Subject(s)
Arabidopsis/genetics , Chromosomes/genetics , DNA, Plant/genetics , Proto-Oncogene Proteins c-myb , Arabidopsis/chemistry , Arabidopsis Proteins , Chromosome Mapping , Cloning, Molecular , DNA, Plant/chemistry , DNA-Binding Proteins/genetics , Gene Expression/genetics , Genes, Plant/genetics , Genome, Plant , MADS Domain Proteins , Molecular Sequence Data , Oxidoreductases/genetics , Phosphotransferases/genetics , Plant Proteins/genetics , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Transcription Factors/genetics
3.
FEBS Lett ; 416(2): 156-60, 1997 Oct 20.
Article in English | MEDLINE | ID: mdl-9369203

ABSTRACT

As part of the European Union program of European Scientist Sequencing Arabidopsis (ESSA), the DNA sequence of a 24.053-bp insert of cosmid clone CC17J13 was determined. The cosmid is located on chromosome 1 at the PFL locus (position 30 cM). Analysis of the sequence and comparison to public databases predicts seven genes in this area, thus approximately one gene every 3.3 kb. Three cDNAs corresponding to genes in this region were also sequenced. The homologies and/or possible functions of the (putative) genes are discussed. Proteins encoded by genes in this region include a polyadenylate-binding protein (PAB-3) and a GTP-binding protein (Rab7) as well as a novel protein, possibly involved in double-stranded RNA unwinding and apoptosis. Intriguingly, the gene encoding the PAB-3 protein, which is very specifically expressed, is flanked by putative matrix attachment regions.


Subject(s)
Arabidopsis/genetics , Chromosome Mapping , rab GTP-Binding Proteins , Base Sequence , DNA, Complementary , DNA, Plant/chemistry , Databases as Topic , Europe , GTP-Binding Proteins/genetics , Genome, Plant , Molecular Sequence Data , Poly(A)-Binding Proteins , RNA-Binding Proteins/genetics , Sequence Analysis, DNA , Sequence Homology, Nucleic Acid , rab7 GTP-Binding Proteins
4.
FEBS Lett ; 372(1): 13-9, 1995 Sep 18.
Article in English | MEDLINE | ID: mdl-7556633

ABSTRACT

A full-length cDNA and the corresponding At-P5S gene encoding the first enzyme of the proline biosynthetic pathway, the delta 1-pyrroline-5-carboxylate (P5C) synthetase, were isolated in Arabidopsis thaliana. The At-P5S cDNA encodes a protein of 717 amino acids showing high identity with the P5C synthetase of Vigna aconitifolia. Strong homology is also found at the N-terminus to bacterial and yeast gamma-glutamyl kinase and at the C-terminus to bacterial gamma-glutamyl phosphate reductase. Putative ATP- and NAD(P)H-binding sites are suggested in the At-P5S protein. The transcribed region of the At-P5S gene is 4.8 kb long and contains 20 exons. Southern analysis suggests the presence of only one At-P5S gene in the A. thaliana genome mapped at the bottom of the chromosome two. Expression analysis of At-P5S in different organs reveals abundant At-P5S transcripts in mature flowering plant. Rapid induction of the At-P5S gene followed by accumulation of proline was observed in NaCl-treated seedlings suggesting that At-P5S is osmoregulated.


Subject(s)
Arabidopsis/genetics , Chromosome Mapping , Genes, Plant , Oxidoreductases Acting on CH-NH Group Donors/genetics , 1-Pyrroline-5-Carboxylate Dehydrogenase , Aldehyde Oxidoreductases/chemistry , Amino Acid Sequence , Arabidopsis/enzymology , Base Sequence , Blotting, Southern , Cloning, Molecular , DNA Primers/chemistry , DNA Primers/genetics , DNA, Complementary/genetics , Gene Expression Regulation, Plant/genetics , Glutamate-5-Semialdehyde Dehydrogenase , Leucine Zippers/genetics , Molecular Sequence Data , Oxidoreductases Acting on CH-NH Group Donors/chemistry , Oxidoreductases Acting on CH-NH Group Donors/metabolism , Phosphotransferases (Carboxyl Group Acceptor)/chemistry , Polymerase Chain Reaction , Proline/biosynthesis , Protein Structure, Secondary , Sequence Alignment , Sodium Chloride/pharmacology , Transcription, Genetic/genetics
5.
Mol Microbiol ; 8(3): 603-13, 1993 May.
Article in English | MEDLINE | ID: mdl-8326868

ABSTRACT

The soil fungus Trichoderma harzianum is a mycoparasitic fungus known for its use as a biocontrol agent of phytopathogenic fungi. Among other factors, Trichoderma produces a series of antibiotics and fungal cell wall-degrading enzymes. These enzymes are believed to play an important role in mycoparasitism. Among the hydrolytic enzymes, we have identified a basic proteinase (Prb1) which is induced by either autoclaved mycelia, fungal cell wall preparation or chitin; however, the induction does not occur in the presence of glucose. The proteinase was purified and biochemically characterized as a serine proteinase of 31 kDa and pI 9.2. Based on the sequence of three internal peptides, synthetic oligonucleotide probes were designed. These probes allowed subsequent isolation of a cDNA and its corresponding genomic clone. The deduced amino acid sequence indicates that the proteinase is synthesized as a pre-proenzyme and allows its classification as a serine proteinase. Northern analysis shows that the induction of this enzyme is due to an increase in the corresponding mRNA level.


Subject(s)
Fungal Proteins , Genes, Fungal , Serine Endopeptidases/genetics , Trichoderma/genetics , Amino Acid Sequence , Base Sequence , Cell Wall/metabolism , Chitin/pharmacology , Consensus Sequence , DNA/genetics , Fungi , Gene Expression Regulation, Fungal/drug effects , Host-Parasite Interactions , Molecular Sequence Data , Open Reading Frames , Protein Sorting Signals/genetics , Sequence Alignment , Sequence Homology, Amino Acid , Serine Endopeptidases/metabolism , Soil Microbiology , Trichoderma/enzymology , Trichoderma/pathogenicity , Virulence/genetics
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