从蓖麻籽胚乳微体中分离出的一种半胱氨酸内肽酶可加工乙醛酸循环体苹果酸脱氢酶前体蛋白。
A cysteine endopeptidase isolated from castor bean endosperm microbodies processes the glyoxysomal malate dehydrogenase precursor protein.
作者信息
Gietl C, Wimmer B, Adamec J, Kalousek F
机构信息
Institute of Botany, Technical University of Munich, Germany.
出版信息
Plant Physiol. 1997 Mar;113(3):863-71. doi: 10.1104/pp.113.3.863.
Abstract
A plant cysteine endopeptidase with a molecular mass of 35 kD was purified from microbodies of germinating castor bean (Ricinus communis) endosperm by virtue of its capacity to specifically process the glyoxysomal malate dehydrogenase precursor protein to the mature subunit in vitro. Processing of the glyoxysomal malate dehydrogenase precursor occurs sequentially in three steps, the first intermediate resulting from cleavage after arginine-13 within the presequence and the second from cleavage after arginine-33. The endopeptidase is unable to remove the presequences of prethiolases from rape (Brassica napus) glyoxysomes and rat peroxisomes at the expected cleavage site. Protein sequence analysis of N-terminal and internal peptides revealed high identity to the mature papain-type cysteine endopeptidases from cotyledons of germinating mung bean (Vigna mungo) and French bean (Phaseolus vulgaris) seeds. These endopeptidases are synthesized with an extended pre-/prosequence at the N terminus and have been considered to be processed in the endoplasmic reticulum and targeted to protein-storing vacuoles.
摘要
从萌发蓖麻（Ricinus communis）胚乳的微体中纯化出一种分子量为35 kD的植物半胱氨酸内肽酶，其依据在于它能够在体外将乙醛酸循环体苹果酸脱氢酶前体蛋白特异性加工成成熟亚基。乙醛酸循环体苹果酸脱氢酶前体的加工依次分三步进行，第一个中间体是在前导序列内精氨酸-13之后切割产生的，第二个中间体是在精氨酸-33之后切割产生的。该内肽酶无法在预期切割位点去除油菜（Brassica napus）乙醛酸循环体和大鼠过氧化物酶体中硫解酶前体的前导序列。对N端和内部肽段的蛋白质序列分析表明，它与萌发绿豆（Vigna mungo）和菜豆（Phaseolus vulgaris）种子子叶中成熟的木瓜蛋白酶型半胱氨酸内肽酶具有高度同源性。这些内肽酶在N端合成时带有一个延长的前导/前体序列，并且被认为在内质网中进行加工并靶向到蛋白质储存液泡。
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