Proteins associated with the Arabidopsis thaliana plastid rhomboid-like protein RBL10.

Autor: Lavell A; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.; DOE-Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA., Smith M; DOE-Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Chemical Engineering and Material Science, Michigan State University, East Lansing, MI, 48824, USA., Xu Y; DOE-Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA., Froehlich JE; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.; DOE-Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA., De La Mora C; DOE-Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Molecular & Cellular Biology, Illinois State University, Normal, IL, 61761, USA., Benning C; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.; DOE-Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Plant Biology, Michigan State University, East Lansing, MI, 488824, USA.
Jazyk: angličtina
Zdroj: The Plant journal : for cell and molecular biology [Plant J] 2021 Dec; Vol. 108 (5), pp. 1332-1345. Date of Electronic Publication: 2021 Oct 15.
DOI: 10.1111/tpj.15514
Abstrakt: Rhomboid-like proteins are intramembrane proteases with a variety of regulatory roles in cells. Though many rhomboid-like proteins are predicted in plants, their detailed molecular mechanisms or cellular functions are not yet known. Of the 13 predicted rhomboids in Arabidopsis thaliana, one, RBL10, affects lipid metabolism in the chloroplast, because in the respective rbl10 mutant the transfer of phosphatidic acid through the inner envelope membrane is disrupted. Here we show that RBL10 is part of a high-molecular-weight complex of 250 kDa or greater in size. Nine likely components of this complex are identified by two independent methods and include Acyl Carrier Protein 4 (ACP4) and Carboxyltransferase Interactor1 (CTI1), which have known roles in chloroplast lipid metabolism. The acp4 mutant has decreased C16:3 fatty acid content of monogalactosyldiacylglycerol, similar to the rbl10 mutant, prompting us to offer a mechanistic model of how an interaction between ACP4 and RBL10 might affect chloroplast lipid assembly. We also demonstrate the presence of a seventh transmembrane domain in RBL10, refining the currently accepted topology of this protein. Taken together, the identity of possible RBL10 complex components as well as insights into RBL10 topology and distribution in the membrane provide a stepping-stone towards a deeper understanding of RBL10 function in Arabidopsis lipid metabolism.
(© 2021 Society for Experimental Biology and John Wiley & Sons Ltd.)
Databáze: MEDLINE
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