Artículo

Goldstein, D.J.; Fondrat, C.; Muri, F.; Nuel, G.; Saragueta, P.; Tocquet, A.-S.; Prum, B. "Short inverse complementary amino acid sequences generate protein complexity" (2003) Comptes Rendus - Biologies. 326(3):339-348
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Abstract:

Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among protein registered in Swiss Prot. The observed number of princoms occurrences exceeds by far the expected number (p < 10-10). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes. © 2003 Académie des sciences/Éditions scientifiques et médicales Elsevier SAS. All rights reserved.

Registro:

Documento: Artículo
Título:Short inverse complementary amino acid sequences generate protein complexity
Autor:Goldstein, D.J.; Fondrat, C.; Muri, F.; Nuel, G.; Saragueta, P.; Tocquet, A.-S.; Prum, B.
Filiación:Departamento de Ciencias Biologicas, Facultad Ciencias Exactas Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Direction des Systemes d'Information, Universite Rene-Descartes Paris-5, 12 rue de l'Ecole-de-Medecine, 75270 Paris Cedex 06, France
Laboratoire Statistique et Genome, Upresa CNRS 8071, Departement de Mathematique, 523 place des Terrasses-de-l'Agora, 91000 Évry, France
Département STID, Inst. Universitaire de Technologie, Académie de Paris, 143 avenue de Versailles, 75016 Paris, France
Departamento de Quimica Biologica, Facultad Ciencias Exactas Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Genomic complexity; Genomic inversions; Inverse complementary; amino acid; disulfide; DNA; messenger RNA; amino acid; genome; protein; amino acid sequence; article; biochemistry; controlled study; disulfide bond; gene sequence; gene structure; protein analysis; protein function; protein motif; sequence database; SWISS-PROT
Año:2003
Volumen:326
Número:3
Página de inicio:339
Página de fin:348
DOI: http://dx.doi.org/10.1016/S1631-0691(03)00077-5
Título revista:Comptes Rendus - Biologies
Título revista abreviado:C. R. Biol.
ISSN:16310691
CODEN:CRBOC
CAS:amino acid, 65072-01-7; disulfide, 16734-12-6; DNA, 9007-49-2
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_16310691_v326_n3_p339_Goldstein

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Citas:

---------- APA ----------
Goldstein, D.J., Fondrat, C., Muri, F., Nuel, G., Saragueta, P., Tocquet, A.-S. & Prum, B. (2003) . Short inverse complementary amino acid sequences generate protein complexity. Comptes Rendus - Biologies, 326(3), 339-348.
http://dx.doi.org/10.1016/S1631-0691(03)00077-5
---------- CHICAGO ----------
Goldstein, D.J., Fondrat, C., Muri, F., Nuel, G., Saragueta, P., Tocquet, A.-S., et al. "Short inverse complementary amino acid sequences generate protein complexity" . Comptes Rendus - Biologies 326, no. 3 (2003) : 339-348.
http://dx.doi.org/10.1016/S1631-0691(03)00077-5
---------- MLA ----------
Goldstein, D.J., Fondrat, C., Muri, F., Nuel, G., Saragueta, P., Tocquet, A.-S., et al. "Short inverse complementary amino acid sequences generate protein complexity" . Comptes Rendus - Biologies, vol. 326, no. 3, 2003, pp. 339-348.
http://dx.doi.org/10.1016/S1631-0691(03)00077-5
---------- VANCOUVER ----------
Goldstein, D.J., Fondrat, C., Muri, F., Nuel, G., Saragueta, P., Tocquet, A.-S., et al. Short inverse complementary amino acid sequences generate protein complexity. C. R. Biol. 2003;326(3):339-348.
http://dx.doi.org/10.1016/S1631-0691(03)00077-5