The Library
Characterisation of an Arabidopsis cDNA encoding a thylakoid lumen protein related to a novel 'pentapeptide repeat' family of proteins
Tools
UNSPECIFIED (1998) Characterisation of an Arabidopsis cDNA encoding a thylakoid lumen protein related to a novel 'pentapeptide repeat' family of proteins. FEBS LETTERS, 428 (3). pp. 241-244. ISSN 0014-5793.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Abstract
We have cloned an Arabidopsis cDNA encoding a novel thylakoid lumen protein, P17.4, that has been previously isolated from lumen extracts of spinach chloroplasts. The protein is synthesised with a bipartite presequence containing a Sec-type Lumen-targeting signal peptide and the precursor protein is imported into the Lumen of pea chloroplasts. The encoded protein is homologous to an Anabaena protein that is essential for correct glycolipid localisation, and is also related to at least 16 unassigned open reading frames in Synechocystis. This family of proteins is characterised by the presence of numerous pentapeptide repeats with the consensus structure AXLXX, and its members are predicted to be located in the cytosol, plasma membrane and periplasm/lumen. P17.4 is therefore the first higher plant member of an extended family of putative cyanobacterial proteins that may serve important roles in lipid transport or assembly. (C) 1998 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 | ||||
Official Date: | 29 May 1998 | ||||
Dates: |
|
||||
Volume: | 428 | ||||
Number: | 3 | ||||
Number of Pages: | 4 | ||||
Page Range: | pp. 241-244 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |