Erdmann R
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.
Yeast. 1994 Jul;10(7):935-44. doi: 10.1002/yea.320100708.
All peroxisomal 3-oxoacyl-CoA thiolases identified so far do not contain the previously identified tripeptide peroxisomal targeting signal at their carboxy-termini. For the two rat thiolases it was shown that their peroxisomal targeting signals are localized within the amino-terminal region of the proteins and are cleaved upon import. This report demonstrates that the N-terminal region of the peroxisomal 3-oxoacyl-CoA thiolase from Saccharomyces cerevisiae is essential for its peroxisomal targeting, and that the N-terminal 16 amino acids of yeast thiolase are sufficient to target the otherwise cytosolic small subunit of ribulose-1,5-bisphosphate carboxylase to peroxisomes for import.
迄今为止所鉴定出的所有过氧化物酶体3-氧代酰基辅酶A硫解酶在其羧基末端均不包含先前鉴定出的三肽过氧化物酶体靶向信号。对于两种大鼠硫解酶，已表明它们的过氧化物酶体靶向信号位于蛋白质的氨基末端区域，并在导入时被切割。本报告表明，酿酒酵母过氧化物酶体3-氧代酰基辅酶A硫解酶的N末端区域对其过氧化物酶体靶向至关重要，并且酵母硫解酶的N末端16个氨基酸足以将原本位于胞质溶胶中的1,5-二磷酸核酮糖羧化酶小亚基靶向过氧化物酶体进行导入。
