Nucleotide sequence data from several pea (Piswn sativum L.) seed storage protein genes was obtained. Of two legumin genes sequenced, one was shown to be a pseudogene, apparently once coding for a polypeptide belonging to the 'major' legumin class, whilst the other was shown to be a functional gene coding for a polypeptide of the 'minor' legumin class. Sequence data was also obtained for two vicilin genes. Complete sequencing of one revealed it to be truncated by sequence of unknown origin at its 3' end, whilst partial sequence for the other suggested the presence of a stop codon in the coding region. These findings implied that both vicilin genes are no longer functional. Additionally, various comparisons of nucleic acid and amino acid sequence data were made between these genes and also with other legume seed storage protein genes. Results showed these genes conform with the major structural features of eukaryotic genes, and also revealed the presence of potential tissue -specific regulatory elements in the 5' flanking regions of the genes. Dendrograms for legume 11S and 7S classes of globulin seed storage protein genes clearly supported the model theory of each class having arisen by successive duplications from a common ancestral gene.

No description available.

The nucleotide sequence for the pDKl TOL plasmid region encoding toluate-1,2-dioxygenase (Xy1XYZ, TO) was determined. TO is the first enzyme in the meta-cleavage operon, responsible for the conversion of toluates and benzoates to their carboxy-substituted diols. DNA sequence analysis revealed the presence of three open reading frames (ORF). The three ORFs correspond to xylX (1353 bp), xylY (486 bp) and xylZ (1008 bp), encoding predicted protein products of 51370 Da, 19368 Da and 36256 Da, respectively.

Thesis (Ph. D.)--Pennsylvania State University, 1992. / Includes bibliographical references.

Carbonic anhydrase is a ubiquitous zinc-metalloenzyme that catalyzes the interconversion of carbon dioxide and carbonate and has been found to play a wide range of roles in animals, plants and bacteria. Cotton genomic and cDNA libraries were screened for the plastidial isoform of carbonic anhydrase. The nucleotide sequences of two 1.2 Kb partial cDNA clones were determined. These clones exhibit high homology to carbonic anhydrases from other dicot plants and possess all the expected peptide motifs. For example, serine and threonine rich chloroplastic targeting peptide and conserved zinc binding residues are both present. These clones were utilized to isolate two carbonic anhydrase genes that were shown to encode different isoforms by PCR and RFLP analysis.

Rhabdoviridae family viruses attacking the plant hosts were only described at the angiosperms. In this work, a gymnosperm rhabdoviridae infection was described for the first time ever ? specifically at Ginkgo biloba. Even though there were not observed any kinds of obvious infection symptoms on any of randomly chosen plant samples, through the molecular methods and detection primers the rhabdoviridae infection was proved at six of the plant samples. The acquired nucleotide and amino acid sequences, which were compared with the GenBank sequences, confirm the Rhabdoviridae family viruses occurrence. These given sequences demonstrated a certain analogy with a Strawberry crinkle virus assigned to the genus of Cytorhabdoviruses. The analyses proved a different reciprocal homology among the nucleotide sequences of the individual isolates, and in all likelihood an occurrence of two up to now unknown viruses in the Ginkgo biloba samples was proved for the first time. A definite categorization will be dependent on an acquisition and comparison of other sequences from the isolates genome and also on certain biological characteristics observation.