Turk Martina, Plemenitas Ana
Institute of Biochemistry, Faculty of Medicine, Vrazov trg 2, SI-1000, Ljubljana, Slovenia.
FEMS Microbiol Lett. 2002 Nov 5;216(2):193-9. doi: 10.1111/j.1574-6968.2002.tb11435.x.
The mitogen-activated protein kinase (MAPK) Hog1p plays an essential role in the yeast hyperosmotic response. A homolog of the HOG1 gene was isolated from the halophilic black yeast Hortaea werneckii encoding a putative 359 amino acid protein, HwHog1p, with high homology to Saccharomyces cerevisiae Hog1p and to other eukaryotic Hog1p homologs. HwHog1p contains a TGY motif within a protein kinase catalytic domain and a C-terminal common docking (CD) motif. Its activation by increased salinity is regulated at the posttranscriptional level. HwHog1p is located on the plasma membrane under nonstress conditions. Upon increased external salinity it is translocated from the membrane, presumably to the nucleus.
丝裂原活化蛋白激酶（MAPK）Hog1p在酵母的高渗应激反应中起着至关重要的作用。从嗜盐黑酵母沃尔内克霍塔酵母中分离出HOG1基因的一个同源物，它编码一种推定的359个氨基酸的蛋白质HwHog1p，与酿酒酵母Hog1p以及其他真核生物Hog1p同源物具有高度同源性。HwHog1p在蛋白激酶催化结构域内含有一个TGY基序和一个C端通用对接（CD）基序。盐度增加对其激活作用在转录后水平受到调控。在非应激条件下，HwHog1p位于质膜上。当外部盐度增加时，它从膜上转移，推测转移至细胞核。
