Premium
Splicing before import – An intein in a mitochondrially targeted preprotein folds and is catalytically active in the cytoplasm in vivo
Author(s) -
Williams Lisa R.,
Ellis Steven R.,
Hopper Anita K.,
Davis Elaine O.,
Martin Nancy C.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01736-1
Subject(s) - intein , cytoplasm , saccharomyces cerevisiae , mitochondrion , organelle , protein splicing , biology , biochemistry , rna splicing , yeast , microbiology and biotechnology , gene , rna
Nuclear‐encoded mitochondrial proteins are cytoplasmically synthesized and imported into the organelle. The intein‐containing RecA protein of Mycobacterium tuberculosis , with or without the CoxIVp mitochondrial targeting signal (MTS), was used to determine where a protein targeted to mitochondria folds and becomes catalytically active. Analysis of fractions from Saccharomyces cerevisiae cells expressing RecA without the MTS revealed that RecA and intein proteins remained cytoplasmic. With the MTS, most of RecA was directed to mitochondria, while most of the intein remained in the cytoplasm. The intein therefore folds into a catalytically active state in the cytoplasm prior to RecA import into mitochondria.