We examined
chlL (
frxC) gene evolution using several approaches. Sequences from the chloroplast genome of the fern
Polystichum acrostichoides and from the cyanobacterium
Synechococcus sp. 7002 were determined and found to be highly conserved. A complete physical map of the fern chloroplast genome and partial maps of other vascular plant taxa show that
chlL is located primarily in the small single copy region as in
Marchantia polymorpha. A survey of a wide variety of non-angiospermous vascular plant DNAs shows that
chlL is widely distributed but has been lost in the pteridophyte
Psilotum and (presumably independently) within the Gnetalean gymnosperms.The name
frxC was originally used to denote a gene encoding a product with probable Fe : S cluster binding activity. This activity was postulated due to the amino acid sequence similarity between this product and the Fe : S-binding nitrogenase iron protein
nifH. Fe : S-binding is a property shared by ferredoxins, which are denoted by the prefix
frx. However, this gene does not encode a ferredoxin. It is much larger than any known ferredoxin, it binds its Fe : S cluster between two halves of a homodimer (
Fujita & al. 1989,
Burke & al. 1993 a, c) instead of within a single subunit, and it lacks the pattern of clustered cysteines present in all ferredoxins (
Meyer 1988). Therefore, we use the name
chlL to recognize the sequence and functional similarities to the bacterial PChlide reductase subunit,
bchL. Similar usage has been adopted for this (
Suzuki & Bauer 1992) and other (
Choquet & al. 1992,
Burke & al. 1993b) PChlide reductase subunits.
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