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Translocation from nuclei to cytoplasm is necessary for anti A‐PCD activity and turnover of the Type II IAP BcBir1
Author(s) -
Shlezinger Neta,
Israeli Maayan,
Mochly Elad,
OrenYoung Liat,
Zhu Wenjun,
Sharon Amir
Publication year - 2016
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13238
Subject(s) - cytoplasm , biology , microbiology and biotechnology , programmed cell death , nucleus , yeast , saccharomyces cerevisiae , apoptosis , inhibitor of apoptosis , biochemistry
Summary T ype II inhibitors of apoptosis ( IAP s) belong to a subgroup of IAP ‐related proteins. While IAPs are restricted to animals, T ype II IAPs are found in other phyla, including fungi. BcB ir1, a T ype II IAP from B otrytis cinerea has anti apoptotic‐like programmed cell death ( A ‐ PCD ) activity, which is important for pathogenicity of this fungus. Here we report on the role of sub‐cellular localization of BcB ir1 in protein turnover and anti A ‐ PCD activity. Expression of BcB ir1 in S accharomyces cerevisiae had no effect on sensitivity of the yeast cells to A ‐ PCD ‐inducing conditions, whereas expression of a truncated N ' part reduced sensitivity of the cells to these conditions. The full‐length BcB ir1 protein was detected only in the yeast nucleus, whereas the N ' part was observed both in the nucleus and cytoplasm. In B . cinerea , BcB ir1 was mainly nuclear under optimal conditions, whereas under A ‐ PCD ‐inducing conditions it shuttled to the cytoplasm and then it was completely degraded. Collectively, our results show that anti A ‐ PCD activity of BcB ir1 occurs in the cytoplasm, the C ′ end mediates regulation of steady state level of BcB ir1 in the nucleus, and the N ' end mediates anti A ‐ PCD activity as well as fast degradation of BcB ir1 in the cytoplasm.