In:
FEBS Letters, Wiley, Vol. 471, No. 2-3 ( 2000-04-14), p. 191-196
Abstract:
We have identified an open reading frame with homology to prokaryotic rubredoxins (rds) on a nucleomorph chromosome of the cryptomonad alga Guillardia theta . cDNA analysis let us propose that the rd preprotein has an NH 2 ‐terminal extension that functions as a transit peptide for import into the plastid. Compared to rds found in non‐photosynthetic prokaryotes or found in bacteria that exhibit an anoxigenic photosynthesis apparatus, nucleomorph rd has a COOH‐terminal extension, which shows high homology exclusively to the COOH‐termini of cyanobacterial rds as well as to a hypothetical rd in the Arabidopsis genome. This extension can be divided into a putative membrane anchor and a stretch of about 20 amino acids with unknown function linking the common rd fold to this anchor. Overexpression of nucleomorph rd in Escherichia coli using a T7 RNA polymerase/promotor system resulted in a mixture of iron‐containing holorubredoxin and zinc‐substituted protein. Preliminary spectroscopic studies of the iron form of nucleomorph rd suggest the existence of a native rd‐type iron site. One‐dimensional nuclear magnetic resonance spectroscopy of recombinant Zn‐rd suggests the presence of a stable tertiary fold similar to that of other rd structures determined previously.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(00)01399-5
Language:
English
Publisher:
Wiley
Publication Date:
2000
detail.hit.zdb_id:
1460391-3
SSG:
12
Permalink