Disease relevance of BCCP/BCCP-1/BCCP1/CAC1-A/CAC1A

• The 3' end of the CAC1 sequence, coding for a peptide of 94 amino acids, which includes a putative biotinylation motif, was expressed in Escherichia coli as a glutathione-S-transferase (GST) fusion protein [1].
• This paper describes the cloning and characterization of a plant biotin carboxyl carrier protein (BCCP) from the type II ACCase complex that shows 61% identity/79% similarity with Anabaena BCCP at the amino acid level [2].

High impact information on BCCP/BCCP-1/BCCP1/CAC1-A/CAC1A

• Both antisense and sense expression of biotin carboxyl carrier protein isoform 2 inactivates the plastid acetyl-coenzyme A carboxylase in Arabidopsis thaliana [3].
• Analysis of 38 independent Arabidopsis lines expressing antisense BCCP2 transcript behind a constitutive promoter showed no significant phenotype, though antisense transcript was highly expressed [3].
• AtBCCP1 protein was present in developing tissues from roots, leaves, flowers, siliques, and seeds, whereas AtBCCP2 protein was primarily expressed in 7 to 10 d-after-flowering seeds at levels approximately 2-fold less abundant than AtBCCP1 [4].
• These data indicate that oilseed plants in the family Brassicaceae contain at least one to three seed-up-regulated BCCP isoforms, depending upon genome complexity [4].
• Subcellular immunogold labeling indicates that the biotin carboxyl-carrier subunit is localized in the stroma of the plastids and chloroplasts [5].

Biological context of BCCP/BCCP-1/BCCP1/CAC1-A/CAC1A

• The deduced amino acid sequence of CAC1 has an apparent N-terminal chloroplast-targeting transit peptide [1].
• CAC1 is a single-copy gene interrupted by six introns [5].
• Northern analysis showed that although the relative levels of BCCP and betaCT mRNA differed between different oilseed rape tissues, their temporal patterns of expression were identical during embryo development [2].
• The BCCP sequences allowed the assignment of function to two previously unassigned Arabidopsis expressed sequence tag (EST) sequences [2].

Associations of BCCP/BCCP-1/BCCP1/CAC1-A/CAC1A with chemical compounds

• These characterizations identify CAC1 as the biotin-containing subunit of the plastidic, heteromeric ACCase of Arabidopsis [1].
• We report the molecular cloning and sequence of the cDNA coding for the biotin-containing subunit of the chloroplastic acetylcoenzyme A (CoA) carboxylase (ACCase) of Arabidopsis thaliana (CAC1) [1].

Other interactions of BCCP/BCCP-1/BCCP1/CAC1-A/CAC1A

• Structure of the CAC1 gene and in situ characterization of its expression. The Arabidopsis thaliana gene coding for the biotin-containing subunit of the plastidic acetyl-coenzyme A carboxylase [5].
• We report and characterize here a second Arabidopsis BCCP (AtBCCP2) cDNA with 42% amino acid identity to AtBCCP1 and 75% identity to a class of oilseed rape (Brassica napus) BCCPs [4].

Analytical, diagnostic and therapeutic context of BCCP/BCCP-1/BCCP1/CAC1-A/CAC1A

• At the protein level, expression of BCCP during embryo development was studied by Western blotting, using affinity-purified anti-biotin polyclonal sera [2].

References