Stravopodis D J, Kyrpides N C
J Mol Evol. 1999 May;48(5):625-7. doi: 10.1007/pl00013155.
Protein-tyrosine dephosphorylation is a major mechanism in cellular regulation. A large number of protein-tyrosine phosphatases is known from Eukarya, and more recently bacterial homologues have also been identified. By employing conserved sequence patterns from both eukaryotic and bacterial protein-tyrosine phosphatases, we have identified three homologous sequences in two of the four complete archaeal genomes. Two hypothetical open reading frames in the genome of Methanococcus jannaschii (MJ0215 and MJECL20) and one in the genome of Pyrococcus horikoshii (PH1732) clearly bear all the conserved residues of this family. No homologues were found in the genomes of Archaeoglobus fulgidus and Methanobacterium thermoautotrophicum. This is the first report of protein-tyrosine phosphatase sequences in Archaea.
蛋白质酪氨酸去磷酸化是细胞调控中的一种主要机制。真核生物中已知有大量的蛋白质酪氨酸磷酸酶，最近也鉴定出了细菌同源物。通过利用真核生物和细菌蛋白质酪氨酸磷酸酶的保守序列模式，我们在四个完整古细菌基因组中的两个中鉴定出了三个同源序列。詹氏甲烷球菌基因组中的两个假定开放阅读框（MJ0215和MJECL20）以及嗜热栖热菌基因组中的一个（PH1732）明显具有该家族的所有保守残基。在嗜热栖热放线杆菌和嗜热自养甲烷杆菌的基因组中未发现同源物。这是古细菌中蛋白质酪氨酸磷酸酶序列的首次报道。
