Search: id:"swepub:oai:DiVA.org:umu-58364" >
The lumenal pentape...
The lumenal pentapeptide repeat proteins TL15 and TL20.3 are novel chaperone-like proteins in the chloroplast lumen of higher plants
-
- Hall, Michael, 1980- (author)
- Umeå universitet,Kemiska institutionen,Wolfgang Schröder
-
- von Sydow, Lotta (author)
- Umeå universitet,Kemiska institutionen
-
- Storm, Patrik, 1966- (author)
- Umeå universitet,Kemiska institutionen
-
show more...
-
- Sauer, Uwe (author)
- Umeå universitet,Kemiska institutionen
-
- Kieselbach, Thomas (author)
- Umeå universitet,Kemiska institutionen
-
- Schröder, Wolfgang (author)
- Umeå universitet,Kemiska institutionen,Umeå Plant Science Centre (UPSC)
-
show less...
-
(creator_code:org_t)
- English.
- Related links:
-
https://urn.kb.se/re...
Abstract
Subject headings
Close
- In the thylakoid lumen of Arabidopsis thaliana, three pentapeptide repeat family proteins of unknown function are localized. Pentapeptide repeat proteins (PRP) are comprised of at least eight tandem repeats of five amino acids of the consensus sequence A(D/N)LXX, which fold into a quadrilateral beta helix structure. Here we have solved the crystal structure of the mature form of the lumenal PRP protein TL15 to 1.3 Å resolution. TL15 is comprised of a main pentapeptide domain, consisting of a total of 19 pentapeptide repeats which form five turns of a beta helix, and a C-terminal alpha helix domain consisting of two alpha helices. The alpha helices form a ‘cap’ at the C-terminal end of the beta helix and are connected by a disulphide bond between the conserved cysteine residues C122 and C142. Furthermore we show that the lumenal PRPs TL15 and TL20.3 can assist in refolding of a chemically denatured substrate in vitro, indicating foldase chaperone activity. The three lumenal PRPs have been previously identified as targets of thioredoxin, and interestingly we observed a greatly increased chaperone activity of TL15 and TL20.3 after reduction of their disulphide bonds. Our results provide the high resolution crystal structure of the TL15 protein and our analysis of chaperone activity suggests that TL15 and TL20.3 may constitute a novel type of redox-regulated molecular chaperones in the chloroplast lumen of higher plants.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Photosynthesis
- Chloroplast lumen
- biokemi
- Biochemistry
Publication and Content Type
- vet (subject category)
- ovr (subject category)
To the university's database