Premium
Peroxisomal plant nitric oxide synthase (NOS) protein is imported by peroxisomal targeting signal type 2 (PTS2) in a process that depends on the cytosolic receptor PEX7 and calmodulin
Author(s) -
Corpas Francisco J.,
Barroso Juan B.
Publication year - 2014
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/j.febslet.2014.04.034
Subject(s) - peroxisome , peroxisomal targeting signal , calmodulin , cytosol , nitric oxide synthase , biochemistry , microbiology and biotechnology , nitric oxide , chemistry , receptor , arabidopsis , biology , enzyme , gene , mutant , organic chemistry
Nitric oxide (NO) production in plant peroxisomes by l ‐arginine‐dependent NO synthase activity has been proven. The PEX5 and PEX7 PTS receptors, which recognize PTS1‐ and PTS2‐containing proteins, are localized in the cytosol. Using AtPex5p and AtPex7p knockdown in Arabidopsis by RNA interference (RNAi) designated as pex5i and pex7i , we found that the l ‐arginine‐dependent protein responsible for NO generation in peroxisomes appears to be imported through an N‐terminal PTS2. Pharmacological analyzes using a calcium channel blocker and calmodulin (CaM) antagonist show that the import of the peroxisomal NOS protein also depends on calcium and calmodulin.
Discover
Journals
Proceedings
Books
Explore
Engineering & Computer Science
Health & Medical Sciences
Humanities, Literature & Arts
Life Sciences & Earth Sciences
Physics & Mathematics
Social Sciences
Chemical & Material Sciences
Business, Economics & Management