一种输入蛋白与莱茵衣藻完整叶绿体及分离的叶绿体被膜的结合。

Binding of an import protein to intact chloroplasts and to isolated chloroplast envelopes of Chlamydomonas reinhardii.

作者信息

Su Q X, Niklaus A, Rothen R, Boschetti A

机构信息

Institute of Biochemistry, University of Bern, Switzerland.

出版信息

FEBS Lett. 1992 Mar 30;300(2):157-61. doi: 10.1016/0014-5793(92)80186-k.

DOI:10.1016/0014-5793(92)80186-k

PMID:1563516

Abstract

The binding affinity of the precursor of the small subunit of ribulose-1,5-bisphosphate carboxylase (pSS) to isolated, intact chloroplasts and to isolated chloroplast envelopes from the green alga Chlamydomonas reinhardii was studied under conditions where no import into chloroplasts occurred. pSS bound to both chloroplasts and envelopes with equally high affinity. The dissociation constants were 5.9 +/- 2.1 x 10(-9) M and 2.9 +/- 1.4 x 10(-9) M, respectively. The number of binding sites per chloroplast was determined to be 8.1 +/- 4.1 x 10(4). Binding of pSS to isolated envelopes or intact chloroplasts was specific with respect to the type of the membrane and the presence of the transit sequence.

摘要

在未发生向叶绿体导入的条件下，研究了1,5-二磷酸核酮糖羧化酶小亚基前体（pSS）与莱茵衣藻分离的完整叶绿体以及分离的叶绿体被膜的结合亲和力。pSS与叶绿体和被膜的结合亲和力同样高。解离常数分别为5.9±2.1×10⁻⁹ M和2.9±1.4×10⁻⁹ M。每个叶绿体的结合位点数确定为8.1±4.1×10⁴。pSS与分离的被膜或完整叶绿体的结合对于膜的类型和转运序列的存在具有特异性。