UNSPECIFIED (2000) Different lumen-targeting pathways for nuclear-encoded versus cyanobacterial/plastid-encoded Hcf136 proteins. FEBS LETTERS, 467 (1). pp. 97-100. ISSN 0014-5793

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Abstract

Lumenal proteins are transported across the thylakoid membrane by two very different pathways: Sec-dependent or tn in-arginine translocase (Tat)-dependent, where the substrate protein can be transported in a folded state. We present the first evidence that a given protein can be targeted by different pathways in different organisms. Arabidopsis Hcf136 is targeted exclusively by the Tat pathway in pea chloroplasts and no Sec-dependent transport is evident even when the twin-arginine is replaced by twin-lysine, However, twin-arginine motifs are absent from the presequences of Hcf136 proteins encoded by plastid or cyanobacterial genomes, strongly implying translocation by another pathway (presumably Sec). We suggest that the Hcf136 protein was transferred to the Tat pathway when the gene became incorporated into the nuclear genome, possibly due to the tighter folding associated with the more involved, posttranslational targeting pathway, (C) 2000 Federation of European Biochemical Societies.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	FEBS LETTERS
Publisher:	ELSEVIER SCIENCE BV
ISSN:	0014-5793
Date:	4 February 2000
Volume:	467
Number:	1
Number of Pages:	4
Page Range:	pp. 97-100
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/13702

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