Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae

6 pages, 4 figures.

Detalles Bibliográficos
Autores: Gamo, Francisco-Javier, Navas, María-Angeles, Blázquez, Miguel Ángel, Gancedo, Carlos, Gancedo, Juana M.
Tipo de recurso: artículo
Fecha de publicación:1994
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/24014
Acceso en línea:http://hdl.handle.net/10261/24014
Access Level:acceso abierto
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spelling Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiaeGamo, Francisco-JavierNavas, María-AngelesBlázquez, Miguel ÁngelGancedo, CarlosGancedo, Juana M.6 pages, 4 figures.Fructose-1,6-bisphosphatase (FruP2ase) from Saccharomyces cerevisiae is rapidly inactivated upon addition of glucose to a culture growing on non-sugar carbon sources. Under the same conditions the FruP2ases from Schizosaccharomyces pombe or Escherichia coli expressed in S. cerevisiae were not affected. A chimaeric protein confaining the first 178 amino acids from the N-terminal half of S. cerevisiae FruP2ase fused to E. coliβ-galactosidase was susceptible to catabolite inactivation. Elimination of a putative destruction box, RAELVNLVG…KK….K., beginning at amino acid 60 did not prevent catabolite inactivation. Similarly a change of the vacuole-targeting sequence QKKLD, amino acids 80–84, to QKNSD did not affect significantly the course of inactivation of β-galactosidase. A fusion protein carrying only the first 138 amino acids from FruP2ase was inactivated at a higher rate than the one carrying the first 178, suggesting the existence of a protective region between amino acids 138 and 178. A fusion protein carrying the first 81 amino acids from FruP2ase was inactivated by glucose at a similar rate to the one carrying the 178 amino acids, but one with only the first 18 amino acids was resistant to catabolite inactivation. Inactivation of FruP2ase in mutants ubr1 that lack a protein required for ubiquitin-dependent proteolysis, or pral that lack vacuolar protease A, proceeded as in a wild type. Our results suggest that at least two domains of FruP2ase may mark β-galactosidase for catabolite inactivation and that FruP2ase can be inactivated by a mechanism independent of transfer to the vacuole.This work was supported by grants PB87-0294 and PB91-0056 from the Dirección General de Investigación Científica y TécnicaPeer reviewedBlackwell Publishing201020101994info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501728556 bytesapplication/pdfhttp://hdl.handle.net/10261/24014reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1111/j.1432-1033.1994.tb18935.xinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/240142026-05-22T06:33:51Z
dc.title.none.fl_str_mv Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
title Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
spellingShingle Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
Gamo, Francisco-Javier
title_short Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
title_full Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
title_fullStr Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
title_full_unstemmed Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
title_sort Catabolite inactivation of heterologous fructose-1,6-bisphosphatases and fructose-1,6-bisphosphatase-β-galactosidase fusion proteins in Saccharomyces cerevisiae
dc.creator.none.fl_str_mv Gamo, Francisco-Javier
Navas, María-Angeles
Blázquez, Miguel Ángel
Gancedo, Carlos
Gancedo, Juana M.
author Gamo, Francisco-Javier
author_facet Gamo, Francisco-Javier
Navas, María-Angeles
Blázquez, Miguel Ángel
Gancedo, Carlos
Gancedo, Juana M.
author_role author
author2 Navas, María-Angeles
Blázquez, Miguel Ángel
Gancedo, Carlos
Gancedo, Juana M.
author2_role author
author
author
author
description 6 pages, 4 figures.
publishDate 1994
dc.date.none.fl_str_mv 1994
2010
2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/24014
url http://hdl.handle.net/10261/24014
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1111/j.1432-1033.1994.tb18935.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 728556 bytes
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dc.publisher.none.fl_str_mv Blackwell Publishing
publisher.none.fl_str_mv Blackwell Publishing
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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