ISSN:
1432-2048
Keywords:
Arabidopsis
;
Chlorophyll biosynthesis
;
Plastid
;
Porphobilinogen deaminase (purification, subcellular location)
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract A recombinant plasmid, pArab8, harbouring the cDNA encoding the mature form of the tetrapyrrole synthesis enzyme porphobilinogen deaminase (EC 4.3.1.8; also known as hydroxymethylbilane synthase) from Arabidopsis thaliana (L.) Heynh. has been constructed, and used to transform Escherichia coli. The porphobilinogen deaminase protein from Arabidopsis was overexpressed in this strain, and purified to homogeneity (3000-fold) with a yield of 20%. Antibodies were raised against the purified plant enzyme, and used in Western blot analysis, immunoprecipitation of enzyme activity and immuno-gold electron microscopy. The results indicate that the enzyme is confined to plastids in both leaves and roots. The implications of this finding for plant tetrapyrrole synthesis are discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00195187