Ruepp A, Eckerskorn C, Bogyo M, Baumeister W
Max-Planck-Institut für Biochemie, Martinsried, Germany.
FEBS Lett. 1998 Mar 20;425(1):87-90. doi: 10.1016/s0014-5793(98)00205-1.
Hitherto the biology of proteolysis in prokaryotes, particularly in archaea, is only poorly understood. We have used the tri-peptide vinyl sulfone inhibitor carboxybenzyl-leucyl-leucyl-leucine vinyl sulfone (Z-L3VS) to study the in vivo function of proteasomes in Thermoplasma acidophilum. Z-L3VS is a potent inhibitor of the Thermoplasma proteasome and is capable of modifying 75 to 80% of the proteasomal beta-subunits in cell cultures. Inhibition of proteasomes has only marginal effects under normal growth conditions. Under heat shock conditions, however, the effects of proteasome inhibition are much more severe, to the extent of complete cell growth arrest. These data suggest that other proteolytic systems may exist that can compensate for the loss of proteasome function in T. acidophilum.
迄今为止，原核生物，特别是古细菌中蛋白质水解的生物学机制仍知之甚少。我们使用了三肽乙烯砜抑制剂羧苄基 - 亮氨酰 - 亮氨酰 - 亮氨酸乙烯砜（Z - L3VS）来研究嗜热栖热菌中蛋白酶体的体内功能。Z - L3VS是嗜热栖热菌蛋白酶体的有效抑制剂，能够修饰细胞培养物中75%至80%的蛋白酶体β亚基。在正常生长条件下，蛋白酶体的抑制作用仅产生轻微影响。然而，在热休克条件下，蛋白酶体抑制的影响要严重得多，甚至导致细胞生长完全停滞。这些数据表明，可能存在其他蛋白水解系统，可以补偿嗜热栖热菌中蛋白酶体功能的丧失。
