Abstract:
:Native cytochrome c (cyt c) has a compact tertiary structure with a hexacoordinated heme iron and functions in electron transport in mitochondria and apoptosis in the cytoplasm. However, the possibility that protein modifications confer additional functions to cyt c has not been explored. Disruption of methionine 80 (M80)-Fe ligation of cyt c under nitrative stress has been reported. To model this alteration and determine if it confers new properties to cyt c, a cyt c mutant (M80A) was constitutively expressed in cells. M80A-cyt c has increased peroxidase activity and is spontaneously released from mitochondria, translocating to the cytoplasm and nucleus in the absence of apoptosis. Moreover, M80A models endogenously nitrated cyt c because nitration of WT-cyt c is associated with its translocation to the cytoplasm and nucleus. Further, M80A cyt c may up-regulate protective responses to nitrative stress. Our findings raise the possibility that endogenous protein modifications that disrupt the M80-Fe ligation (such as tyrosine nitration) stimulate nuclear translocation and confer new functions to cyt c in nonapoptotic cells.
journal_name
Proc Natl Acad Sci U S Aauthors
Godoy LC,Muñoz-Pinedo C,Castro L,Cardaci S,Schonhoff CM,King M,Tórtora V,Marín M,Miao Q,Jiang JF,Kapralov A,Jemmerson R,Silkstone GG,Patel JN,Evans JE,Wilson MT,Green DR,Kagan VE,Radi R,Mannick JBdoi
10.1073/pnas.0809279106subject
Has Abstractpub_date
2009-02-24 00:00:00pages
2653-8issue
8eissn
0027-8424issn
1091-6490pii
0809279106journal_volume
106pub_type
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