RESUMO
The Gene Ontology (GO) project (http://www. geneontology.org/) provides structured, controlled vocabularies and classifications that cover several domains of molecular and cellular biology and are freely available for community use in the annotation of genes, gene products and sequences. Many model organism databases and genome annotation groups use the GO and contribute their annotation sets to the GO resource. The GO database integrates the vocabularies and contributed annotations and provides full access to this information in several formats. Members of the GO Consortium continually work collectively, involving outside experts as needed, to expand and update the GO vocabularies. The GO Web resource also provides access to extensive documentation about the GO project and links to applications that use GO data for functional analyses.
Assuntos
Bases de Dados Genéticas , Genes , Terminologia como Assunto , Animais , Bibliografias como Assunto , Correio Eletrônico , Genômica , Humanos , Armazenamento e Recuperação da Informação , Internet , Biologia Molecular , Proteínas/classificação , Proteínas/genética , SoftwareRESUMO
During its development, a plant shoot progresses from a juvenile to an adult phase of vegetative growth and from a reproductively incompetent to a reproductively competent state. In Arabidopsis, loss-of-function mutations in SQUINT (SQN) reduced the number of juvenile leaves and had subtle effects on inflorescence morphology but had no effect on flowering time or on reproductive competence. SQN encodes the Arabidopsis homolog of cyclophilin 40 (CyP40), a protein found in association with the Hsp90 chaperone complex in yeast, mammals, and plants. Thus, in Arabidopsis, CyP40 is specifically required for the vegetative but not the reproductive maturation of the shoot.
Assuntos
Arabidopsis/crescimento & desenvolvimento , Arabidopsis/genética , Ciclofilinas , Sequência de Aminoácidos , Arabidopsis/anatomia & histologia , Arabidopsis/fisiologia , Proteínas de Transporte/química , Proteínas de Transporte/genética , Proteínas de Transporte/fisiologia , Mapeamento Cromossômico , Peptidil-Prolil Isomerase F , Éxons , Regulação da Expressão Gênica de Plantas , Genes de Plantas , Proteínas de Choque Térmico/genética , Dados de Sequência Molecular , Mutação , Peptidilprolil Isomerase/química , Peptidilprolil Isomerase/genética , Peptidilprolil Isomerase/fisiologia , Fenótipo , Folhas de Planta/anatomia & histologia , Folhas de Planta/crescimento & desenvolvimento , Brotos de Planta/crescimento & desenvolvimento , Brotos de Planta/fisiologia , Reprodução , Alinhamento de Sequência , TemperaturaRESUMO
The comparison of three complete aldolase B genes-including known and putative regulatory elements-is presented. The third aldolase B gene was provided by the complete aldB gene sequence (14803 bp) encoding the rabbit aldolase B isozyme. The promoter sequence alignment included the nonmammalian chicken aldolase B gene and confirms the promoter sequence conservation of those elements where trans-factor binding has been demonstrated in rat aldB. Moreover, the alignment reveals conserved sequences that may represent previously unidentified promoter elements that are present in all aldBs or specifically in the mammalian aldB promoters. One remarkable feature is a poly-purine segment found between the CAAT and TATA elements. In the mammalian promoters, this is exclusively a 9-10 bp poly-dA stretch. The avian promoter has an additional stretch of eight dG-bases immediately upstream of the poly-dA. Alignment of a portion of intron 1 of the chicken, human, and rabbit aldB genes reveals conserved sequences that are likely candidates for a reported positive activation sequence. In addition, the amino acid sequences of all eight known aldolase B isozymes is compared to the other vertebrate aldolases. A number of aldolase B-specific residues are identified that cluster in the carboxyl-portion of the sequence. With the exception of residue C268, these residues are not found near the active site, although, they are likely to be responsible for the substrate specificity of aldolase B.
Assuntos
Carboxiliases/genética , Frutose-Bifosfato Aldolase/genética , Isoenzimas , Regiões Promotoras Genéticas , Sequência de Aminoácidos , Animais , Northern Blotting , Galinhas , Biblioteca Genômica , Humanos , Modelos Genéticos , Modelos Moleculares , Dados de Sequência Molecular , Coelhos , Ratos , Mapeamento por Restrição , Análise de Sequência de DNA , Homologia de Sequência de AminoácidosRESUMO
A 2061 bp cDNA encoding a goldfish (Carassius auratus) aldolase was isolated from a goldfish brain library. The deduced 362 amino acid sequence is more similar to vertebrate brain (aldolase C) and muscle aldolases (aldolase A) than to the liver isozymes (aldolase B). Northern blot analysis indicates strong expression of the mRNA in brain but not in liver or muscle, which indicates that this is aldolase C rather than aldolase A. Analysis of all known vertebrate aldolase amino acid sequences reveals five residues; Leu-57, Arg-314, Thr-324, Glu-332, and Gly-350 that are present exclusively in aldolase Cs. The goldfish clone possesses all five residues. The residues are primarily located in the carboxyl-terminal region of the enzyme and may play a role in determining the neuronal isozyme-specific properties of the enzyme. Furthermore, the existence of an aldolase C in a teleost fish has implications with respect to the timing of genome duplication events that are thought to have been critical in vertebrate evolution.
