The mitochondrial proteins AtHscB and AtIsu1 involved in Fe-S cluster assembly interact with the Hsp70-type chaperon AtHscA2 and modulate its catalytic activity

被引:27
作者
Leaden, Laura [1 ]
Busi, Maria V. [1 ]
Gomez-Casati, Diego F. [1 ]
机构
[1] Univ Nacl Rosario, Ctr Estudios Fotosintet & Bioquim CEFOBI CONICET, RA-2000 Rosario, Santa Fe, Argentina
关键词
Hsp70-like; Fe-S clusters; Arabidopsis; Mitochondria; IRON-SULFUR CLUSTERS; SCAFFOLD PROTEIN; IN-VIVO; CYSTEINE DESULFURASE; BIOGENESIS; FRATAXIN; ISCU; HSC20; ISU; BIOSYNTHESIS;
D O I
10.1016/j.mito.2014.11.002
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Arabidopsis plants contain two genes coding for mitochondrial Hsp70-type chaperon-like proteins, AtHscA1 (At4g37910) and AtHscA2 (At5g09590). Both genes are homologs of the Ssq1 gene involved in Fe-S cluster assembly in yeast. Protein-protein interaction studies showed that AtHscA2 interacts with AtIsu1 and AtHscB, two Arabidopsis homologs of the Isu1 protein and the Jac1 yeast co-chaperone. Moreover, this interaction could modulate the activity of AtHscA2. In the presence of a 1:5:5 molar ratio of AtHscA2:AtIsu1:AtHscB we observed an increase in the V-max and a decrease in the S-0.5 for ATP of AtHscA2. Furthermore, an increase of about 28-fold in the catalytic efficiency of AtHscA2 was also observed. Results suggest that AtHscA2 in cooperation with AtIsu1 and AtHscB play an important role in the regulation of the Fe-S assembly pathway in plant mitochondria. (C) 2014 Elsevier B.V. and Mitochondria Research Society. All rights reserved.
引用
收藏
页码:375 / 381
页数:7
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