caa a22 4500 477100929 CHVBK 20180405111541.0 cr unu---uuuuu 170330e19960401xx s 000 0 eng 10.1007/BF00262637 doi (NATIONALLICENCE)springer-10.1007/BF00262637 Co-purification, co-imniunoprecipitation, and coordinate expression of acetyl-coenzyme A carboxylase activity, biotin carboxylase, and biotin carboxyl carrier protein of higher plants [Elektronische Daten] [Keith Roesler, Linda Savage, David Shintani, Basil Shorrosh, John Ohlrogge] Acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) is a regulatory enzyme of fatty acid synthesis, and in some higher-plant plastids is a multi-subunit complex consisting of biotin carboxylase (BC), biotin-carboxyl carrier protein (BCCP), and carboxyl transferase (CT). We recently described a Nicotiana tabacum L. (tobacco) cDNA with a deduced amino acid sequence similar to that of prokaryotic BC. We here provide further biochemical and immunological evidence that this higher-plant polypeptide is an authentic BC component of ACCase. The BC protein co-purified with ACCase activity and with BCCP during gel permeation chromatography of Pisum sativum L. (pea) chloroplast proteins. Antibodies to the Ricinus communis L. (castor) BC co-precipitated ACCase activity and BCCP. During castor seed development, ACCase activity and the levels of BC and BCCP increased and subsequently decreased in parallel, indicating their coordinate regulation. The BC protein comprised about 0.8% of the soluble protein in developing castor seed, and less than 0.05% of the protein in young leaf or root. Polypeptides cross-reacting with antibodies to castor BC were detected in several dicotyledons and in the monocotyledons Hemerocallis fulva L. (day lily), Iris L., and Allium cepa L. (onion), but not in the Gramineae species Hordeum vulgare L. (barley) and Panicum virgatum L. (switchgrass). The castor endosperm and pea chloroplast ACCases were not significantly inhibited by long-chain acyl-acyl carrier protein, free fatty acids or acyl carrier protein. The BC polypeptide was detected throughout Brassica napus L. (rapeseed) embryo development, in contrast to the multi-functional ACCase isoenzyme which was only detected early in development. These results firmly establish the identity of the BC polypeptide in plants and provide insight into the structure, regulation and roles of higherplant ACCases. Springer-Verlag, 1996 Acetyl-coenzyme A carboxylase nationallicence Biotin carboxylase nationallicence Fatty acid synthesis nationallicence Brassica (fatty acids) nationallicence Ricinus (fatty acids) nationallicence ACCase : acetyl-CoA carboxylase nationallicence ACP : acyl carrier protein nationallicence BC : biotin carboxylase nationallicence BCCP : biotin carboxyl carrier protein nationallicence CT : carboxyl transferase nationallicence MF : multi-functional nationallicence MS : multi-subunit nationallicence Roesler Keith Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut Savage Linda Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut Shintani David Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut Shorrosh Basil Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut Ohlrogge John Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut Planta Springer-Verlag 198/4(1996-04-01), 517-525 0032-0935 198:4<517 1996 198 425 https://doi.org/10.1007/BF00262637 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00262637 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Roesler Keith Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut NATIONALLICENCE 700 1- Savage Linda Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut NATIONALLICENCE 700 1- Shintani David Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut NATIONALLICENCE 700 1- Shorrosh Basil Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut NATIONALLICENCE 700 1- Ohlrogge John Department of Botany and Plant Pathology, Michigan State University, 48824, East Lansing, MI, USA aut NATIONALLICENCE 773 0- Planta Springer-Verlag 198/4(1996-04-01), 517-525 0032-0935 198:4<517 1996 198 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer