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1.
J Biomol Struct Dyn ; 31(11): 1293-300, 2013.
Artículo en Inglés | MEDLINE | ID: mdl-23140233

RESUMEN

The conserved protein sequence motifs present in all prokaryotic proteomes, "omnipresent motifs," presumably, correspond to the earliest proteins of the Last Universal Cellular Ancestor, from which all the proteomes have descended. Fifteen proteomes, each representing one of the total 15 diverse phyla of 131 Eubacteria and Archea, from which the omnipresent elements have been originally derived, are exhaustively screened. All those proteins which harbor the omnipresent motifs are identified. Six "omnipresent" protein types are revealed which are located in all 15 proteomes: ABC cassettes, FtsH proteases, translation initiation factors, translation elongation factors, isoleucyl-tRNA synthases, and RNA polymerases ß'. In addition to the omnipresent motifs, these proteins also contain other highly conserved motifs, standing for additional modules of the proteins. Remarkably, the identified tentative earliest proteins are responsible for only three basic functions: supply of monomers (ABC transporters and proteases), protein synthesis (initiation and elongation factors, aminoacyl-tRNA synthases), and RNA synthesis (polymerases). No enzymes involved in metabolic activities are present in the list of the earliest proteins derived by this approach. Some of the omnipresent sequence motifs are found, indeed, in the metabolic enzymes (e.g. NTP binding motifs), but these enzymes do not make a sequence matching collection of 15 sequences, i.e. they are not omnipresent. Future analysis of less conserved sequence motifs may reveal at what degree of conservation (stage of evolution) the metabolic enzymes could have entered the scene.


Asunto(s)
Proteínas Arqueales/química , Proteínas Bacterianas/química , Proteoma/química , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Proteínas Arqueales/fisiología , Proteínas Bacterianas/fisiología , Secuencia Conservada , Evolución Molecular , Datos de Secuencia Molecular , Biosíntesis de Proteínas , Proteoma/fisiología , ARN/biosíntesis
2.
J Mol Evol ; 45(3): 271-7, 1997 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-9302321

RESUMEN

Linguistic similarities and dissimilarities between 5 S rRNA sequences allowed taxonomical separation of species and classes. Comparisons with the molecule from mammals distinguished fungi and plants from protists and animals. Similarities to mammalians progressively increased from protists to invertebrates and to somatic-type molecules of the vertebrates lineage. In this, deviations were detected in avian, oocyte type, and pseudogene sequences. Among bacteria, actinobacteria were most similar to the mammalians, which could be related to the high frequency of associations among members of these groups. Some archaebacterial species most similar to the mammalians belonged to the Thermoproteales and Halobacteria groups. Comparisons with the soybean mitochondrial molecule revealed high internal homogeneity among plant mitochondria. The eubacterial groups most similar to it were Thermus and Rhodobacteria gamma-1 and alpha-2. Other procedures have already indicated similarities of Rhodobacteria alpha to mitochondria but the linguistic similarities were on the average higher with the first two groups.


Asunto(s)
ADN Mitocondrial/genética , Mamíferos/genética , Modelos Genéticos , ARN Ribosómico 5S/clasificación , Animales , Bacterias/genética , Células Eucariotas , Hongos/genética , Filogenia , Plantas/genética , Sensibilidad y Especificidad , Glycine max/genética
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