The Thimann Laboratories, University of California, Santa Cruz, California 95064.
Plant Physiol. 1985 Jun;78(2):315-9. doi: 10.1104/pp.78.2.315.
The mechanism whereby l-serine specifically promotes the dark senescence of detached oat (Avena) leaves has been examined. The fact that this promotion is strong in darkness but very weak in white light has been explained, at least in part, by the finding that added serine is partly converted to reducing sugars in light. Labeled serine gives rise to (14)C-sugars and (14)CO(2). In the absence of CO(2), serine does cause chlorophyll loss in light and undergoes a decreased conversion to sugar.As to the large promotion of protease activity which accompanies senescence in the dark, reported earlier, careful purification of the proteases shows that the l-[(14)C]serine is not incorporated into these enzymes, although it is incorporated into the total protein. Cycloheximide decreases the overall synthesis both of protease and of total protein, but again [(14)C]serine does not impart radioactivity to the purified acid proteases. Even when serine is simply added to the protease assay the proteolysis is significantly increased. It is concluded that serine promotes the protease activity by synergizing with the enzyme, or by activating an apoenzyme.
我们研究了 l-丝氨酸促进燕麦离体叶片暗衰老的机制。该促进作用在黑暗中很强,但在白光中很弱,这一事实至少部分可以通过以下发现来解释:添加的丝氨酸在光下部分转化为还原糖。标记的丝氨酸产生 (14)C-糖和 (14)CO(2)。在没有 CO(2)的情况下,丝氨酸确实会在光下导致叶绿素损失,并减少转化为糖。至于先前报道的暗衰老伴随的蛋白酶活性的大量促进,仔细纯化蛋白酶表明,l-[(14)C]丝氨酸未掺入这些酶中,尽管它掺入了总蛋白中。环己酰亚胺降低了蛋白酶和总蛋白的整体合成,但 [(14)C]丝氨酸仍未赋予纯化的酸性蛋白酶放射性。即使将丝氨酸简单地添加到蛋白酶测定中,蛋白水解作用也会显著增加。因此,丝氨酸通过与酶协同作用或激活脱辅基酶来促进蛋白酶活性。