The phosphatidic acid binding site of the arabidopsis trigalactosyldiacylglycerol 4 (TGD4) protein required for lipid import into chloroplasts

Zhen Wang; Nicholas Scott Anderson; Christoph Benning

doi:10.1074/jbc.M112.438986

The phosphatidic acid binding site of the arabidopsis trigalactosyldiacylglycerol 4 (TGD4) protein required for lipid import into chloroplasts

Zhen Wang
, Nicholas Scott Anderson
, Christoph Benning

Biological Sciences

Michigan State University
Dartmouth College

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

Abstract

Background: The phosphatidic acid (PtdOH) binding site of TGD4 is not yet known. Results: Amino acids 1-80 and 110-145 of TGD4 represent two PtdOH interacting sequences and TGD4 forms a homodimer in vitro and in vivo. Conclusion: TGD4 N terminus binds PtdOH while its C terminus interacts with a second TGD4 protein. Significance: This work reveals the structural functional relationship of an essential chloroplast β-barrel lipid transfer protein.

Original language	English
Pages (from-to)	4763-4771
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	7
DOIs	https://doi.org/10.1074/jbc.M112.438986
State	Published - Feb 15 2013

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title = "The phosphatidic acid binding site of the arabidopsis trigalactosyldiacylglycerol 4 (TGD4) protein required for lipid import into chloroplasts",

abstract = "Background: The phosphatidic acid (PtdOH) binding site of TGD4 is not yet known. Results: Amino acids 1-80 and 110-145 of TGD4 represent two PtdOH interacting sequences and TGD4 forms a homodimer in vitro and in vivo. Conclusion: TGD4 N terminus binds PtdOH while its C terminus interacts with a second TGD4 protein. Significance: This work reveals the structural functional relationship of an essential chloroplast β-barrel lipid transfer protein.",

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AU - Anderson, Nicholas Scott

AU - Benning, Christoph

PY - 2013/2/15

Y1 - 2013/2/15

N2 - Background: The phosphatidic acid (PtdOH) binding site of TGD4 is not yet known. Results: Amino acids 1-80 and 110-145 of TGD4 represent two PtdOH interacting sequences and TGD4 forms a homodimer in vitro and in vivo. Conclusion: TGD4 N terminus binds PtdOH while its C terminus interacts with a second TGD4 protein. Significance: This work reveals the structural functional relationship of an essential chloroplast β-barrel lipid transfer protein.

AB - Background: The phosphatidic acid (PtdOH) binding site of TGD4 is not yet known. Results: Amino acids 1-80 and 110-145 of TGD4 represent two PtdOH interacting sequences and TGD4 forms a homodimer in vitro and in vivo. Conclusion: TGD4 N terminus binds PtdOH while its C terminus interacts with a second TGD4 protein. Significance: This work reveals the structural functional relationship of an essential chloroplast β-barrel lipid transfer protein.

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DO - 10.1074/jbc.M112.438986

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The phosphatidic acid binding site of the arabidopsis trigalactosyldiacylglycerol 4 (TGD4) protein required for lipid import into chloroplasts

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