Mullineaux P M, Karpinski S, Jiménez A, Cleary S P, Robinson C, Creissen G P
John Innes Centre, Colney, UK.
Plant J. 1998 Feb;13(3):375-9. doi: 10.1046/j.1365-313x.1998.00052.x.
A cDNA was isolated from pea leaf RNA which encodes a phospholipid hydroperoxide glutathione peroxidase (PHGPX; E.C. 1.1.1.1.9). The N-terminal section of this PHGPX encodes a recognisable chloroplast transit peptide. Efficient import in vitro of the pre-PHGPX protein into the stroma of isolated pea chloroplasts confirmed that the PHGPX is a chloroplast-located enzyme. The pea PHGPX has highly conserved homologues in Arabidopsis, citrus and Nicotiana sylvestris and the authors suggest that these proteins are also localised in the chloroplast and not in the cytosol as previously supposed.
从豌豆叶片RNA中分离出一个cDNA，它编码一种磷脂氢过氧化物谷胱甘肽过氧化物酶（PHGPX；E.C. 1.1.1.1.9）。这种PHGPX的N端部分编码一个可识别的叶绿体转运肽。体外将前体PHGPX蛋白有效导入分离的豌豆叶绿体基质中，证实PHGPX是一种定位于叶绿体的酶。豌豆PHGPX在拟南芥、柑橘和野生烟草中有高度保守的同源物，作者认为这些蛋白质也定位于叶绿体中，而不是如先前推测的定位于细胞质中。
