THE CLEAVABLE PRE-SEQUENCE OF AN IMPORTED CHLOROPLAST PROTEIN DIRECTS ATTACHED POLYPEPTIDES INTO YEAST MITOCHONDRIA
THE CLEAVABLE PRE-SEQUENCE OF AN IMPORTED CHLOROPLAST PROTEIN DIRECTS ATTACHED POLYPEPTIDES INTO YEAST MITOCHONDRIA
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DOI:
10.1002/j.1460-2075.1986.tb04365.x
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发表时间:
1986-06-01
期刊:
影响因子:
11.4
通讯作者:
SCHATZ, G
中科院分区:
文献类型:
--
作者:
HURT, EC;SOLTANIFAR, N;SCHATZ, G
The cleavable pre-sequences of imported chloroplast and mitochondrial protins have several features in common. This structural similarity prompted us to test whether a chloroplast pre-sequence (''transit peptide'') can also be dtcoded by the mitochondrial import machinery. In the green alga, Chlamydomonas reinhardtii, the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (a chloroplast protein) is nuclear-encoded and synthesized in the cytosol with a transient pre-sequence of 45 residues. The 31 amino-terminal residues of this chloroplast pre-sequence were fused to mouse dihydrofolate reductase (a cystolic protein) and to yest cytochrome oxidase subunit IV (an imported mitochondrial protein) from which the authentic pre-sequence had been removed. The chloroplast pre-sequence transported both attached proteins into the yeast mitochondrial matrix or inner membrane, although it functioned less efficiently than an authentic mitochondrial pre-sequence. We conclude that mitochondrial and chloroplast pre-sequences perform their function by a similar mechanism.