Unknown

Dataset Information

0

Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.


ABSTRACT: cDNA fragments encoding part of wheat (Triticum aestivum) acetyl-CoA carboxylase (ACC; EC 6.4.1.2) were cloned by PCR using primers based on the alignment of several biotin-dependent carboxylases. A set of overlapping clones encoding the entire wheat ACC was then isolated by using these fragments as probes. The cDNA sequence contains a 2257-amino acid reading frame encoding a 251-kDa polypeptide. The amino acid sequence of the most highly conserved domain, corresponding to the biotin carboxylases of prokaryotes, is 52-55% identical to ACC of yeast, rat, and diatom. Identity with the available C-terminal amino acid sequence of maize ACC is 66%. The biotin attachment site has the typical eukaryotic EVMKM sequence. The cDNA does not encode an obvious chloroplast targeting sequence. Various cDNA fragments hybridize in Northern blots to a 7.9-kb mRNA. Southern analysis with cDNA probes revealed multiple hybridizing fragments in hexaploid wheat DNA. Some of the wheat cDNA probes also hybridize with ACC-specific DNA from other plants, indicating significant conservation among plant ACCs.

SUBMITTER: Gornicki P 

PROVIDER: S-EPMC44297 | BioStudies | 1994-01-01T00:00:00Z

SECONDARY ACCESSION(S): J03541

REPOSITORIES: biostudies

Similar Datasets

1997-01-01 | S-EPMC28453 | BioStudies
1000-01-01 | S-EPMC44080 | BioStudies
2012-01-01 | S-EPMC3265863 | BioStudies
1999-01-01 | S-EPMC23957 | BioStudies
1000-01-01 | S-EPMC5126230 | BioStudies
2000-01-01 | S-EPMC110990 | BioStudies
1000-01-01 | S-EPMC204996 | BioStudies
1000-01-01 | S-EPMC41997 | BioStudies
2015-01-01 | S-EPMC4838907 | BioStudies
2008-01-01 | S-EPMC2662232 | BioStudies