The physical state of lipid substrates provides transacylation specificity for tafazzin.
The physical state of lipid substrates provides transacylation specificity for tafazzin.
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DOI:
10.1038/nchembio.1064
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发表时间:
2012-10
影响因子:
14.8
通讯作者:
Epand, Richard M.
中科院分区:
文献类型:
--
作者:
Schlame, Michael;Acehan, Devrim;Berno, Bob;Xu, Yang;Valvo, Salvatore;Ren, Mindong;Stokes, David L.;Epand, Richard M.
Cardiolipin is a mitochondrial phospholipid with a characteristic acyl chain composition that depends on the function of tafazzin, a phospholipid-lysophospholipid transacylase, although the enzyme itself lacks acyl specificity. We incubated isolated tafazzin with various mixtures of phospholipids and lysophospholipids, characterized the lipid phase by 31P-NMR, and measured newly formed molecular species by mass spectrometry. Significant transacylation was observed only in non-bilayer lipid aggregates and the substrate specificity was highly sensitive to the lipid phase. In particular, tetralinoleoyl-cardiolipin, a prototype molecular species, formed only under conditions that favor the inverted hexagonal phase. In isolated mitochondria, <1 percent of lipids participated in transacylations, suggesting that the action of tafazzin is limited to privileged lipid domains. We propose that tafazzin reacts with non-bilayer type lipid domains that occur in curved or hemifused membrane zones, and that acyl specificity is driven by the packing properties of these domains.
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影响因子:
4.8
作者:
Acehan, Devrim;Vaz, Frederic;Khuchua, Zaza
通讯作者:
Khuchua, Zaza
影响因子:
30.8
作者:
Bione, S;DAdamo, P;Toniolo, D
通讯作者:
Toniolo, D
DOI:
10.1016/0005-2736(82)90047-5
发表时间:
1982-01-01
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
作者:
DEKRUIJFF, B;NAYAR, R;CULLIS, PR
通讯作者:
CULLIS, PR
影响因子:
3.4
作者:
OTTEN, D;LOBBECKE, L;BEYER, K
通讯作者:
BEYER, K
影响因子:
3.4
作者:
Schlame, Michael;Blais, Steven;Neubert, Thomas A.
通讯作者:
Neubert, Thomas A.