ArticlePlant direct2025
Solution Structure and NMR Chemical Shift Perturbations of the Arabidopsis BCCP1 Identify Intersubunit Interactions Potentially Involved in the Assembly of the Heteromeric Acetyl-CoA Carboxylase.
Article in Plant direct, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Understanding the dynamic nature of plant lipid anabolic and catabolic metabolism is key to sustainable oilseed engineering.The New phytologist · 2026Review
- PII interactions with the acetyl-CoA carboxylase subunits BADC and BCCP co-regulate lipid and nitrogen metabolism in Arabidopsis.Plant physiology · 2025Article
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Authors and funding
4 authors.
Funding
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Abstract
Biotin carboxyl carrier protein (BCCP) is a subunit of the heteromeric acetyl-CoA carboxylase (htACCase), and it chemically links the two half-reactions that constitute the formation of malonyl-CoA from acetyl-CoA, a critical reaction in fatty acid biosynthesis. Because plants are a major source of edible fats and oils, it is important to understand the structural organization of the plant htACCase, relative to its potential to regulate fatty acid biosynthesis in plant plastids. Moreover, unique to the plant htACCase, noncatalytic subunits called biotin attachment domain-containing (BADC) proteins are important in the assembly of the holoenzyme, and they specifically interact with the bcCP and the biotin carboxylase (BC) subunits. We report herein NMR structural studies of the Arabidopsis BCCP isozymes (bcCP1 and BCCP2). We calculated the structure of C-terminal domain of BCCP1 (K
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