| Autor: |
Negrete-Urtasun, Susana, Reiter, Wolfgang, Diez, Eliecer, Denison, Steven H, Tilburn, Joan, Espeso, Eduardo A, Peñalva, Miguel A, Arst, Jr, Herbert N |
| Předmět: |
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| Zdroj: |
Molecular Microbiology; Sep99, Vol. 33 Issue 5, p994-1003, 10p, 7 Diagrams, 1 Graph |
| Abstrakt: |
Completing the molecular analysis of the six pal genes of the ambient pH signal transduction pathway in Aspergillus nidulans , we report the characterization of palC and palH . The derived translation product of palH contains 760 amino acids with prediction of seven transmembrane domains in its N-terminal moiety. Remarkably, a palH frameshift mutant lacking just over half the PalH protein, including almost all of the long hydrophilic region C-terminal to the transmembrane domains, retains some PalH function. The palC -derived translation product contains 507 amino acids, and the null phenotype of a frameshift mutation indicates that at least one of the C-terminal 142 residues is essential for function. Uniquely among the A. nidulans pH-signalling pal genes, palC appears to have no Saccharomyces cerevisiae homologue, although it does have a Neurospora crassa expressed sequence tag homologue. In agreement with findings for the palA , palB and palI genes of this signalling pathway, levels of the palC and palH mRNAs do not appear to be pH regulated. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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