Linked Life Data

10491171

Source:http://linkedlifedata.com/resource/pubmed/id/10491171

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-11-22
pubmed:abstractText
A synthetic peptide MQVTMKSSAVSGQRVGGARVATRSVRRAQLQV corresponding to the 32 amino acid chloroplast transit sequence of the ribulose bisphosphatase carboxylase/oxygenase activase preprotein from Chlamydomonas reinhardtii, required for translocation through the envelope of the chloroplast, has been characterized structurally using CD and NMR under the same experimental conditions as used previously for the 32 amino acid presequence of preferredoxin from the same organism [Lancelin, J.-M., Bally, I., Arlaud, G. J., Blackledge, M., Gans, P., Stein, M. & Jacquot, J.-P. (1994) FEBS Lett. 343, 261-266]. The peptide is found to undergo a conformational transition in aqueous 2,2,2-trifluoroethanol, characterized by three turns of amphiphilic alpha-helix in the C-terminal region preceded by a disordered coil in the N-terminal region. Compared with the preferredoxin transit peptide, the helical and coiled domains are arranged in the reverse order along the peptide sequence, but the positively charged groups are distributed analogously as well as the hydrophobic residues within the amphiphilic alpha-helix. It is proposed that such coil-helix or helix-coil motifs, occasionally repeated, could be an intrinsic structural feature of chloroplastic transit peptides, adapted to the proper translocase and possibly to each nuclear-encoded chloroplast preproteins. This feature may distinguish chloroplastic transit sequences from the other organelle-targeting peptides in the eukaryotic green alga C. reinhardtii, particularly the mitochondrial transit sequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-80
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:10491171-Amino Acid Sequence, pubmed-meshheading:10491171-Animals, pubmed-meshheading:10491171-Biological Transport, pubmed-meshheading:10491171-Chlamydomonas reinhardtii, pubmed-meshheading:10491171-Chloroplasts, pubmed-meshheading:10491171-Circular Dichroism, pubmed-meshheading:10491171-Enzyme Activators, pubmed-meshheading:10491171-Ferredoxins, pubmed-meshheading:10491171-Mass Spectrometry, pubmed-meshheading:10491171-Models, Molecular, pubmed-meshheading:10491171-Molecular Chaperones, pubmed-meshheading:10491171-Molecular Sequence Data, pubmed-meshheading:10491171-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:10491171-Plant Proteins, pubmed-meshheading:10491171-Protein Precursors, pubmed-meshheading:10491171-Protein Sorting Signals, pubmed-meshheading:10491171-Protein Structure, Secondary
pubmed:year
1999
pubmed:articleTitle
A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii.
pubmed:affiliation
Laboratoire de RMN Biomoléculaire associé au CNRS, Université Claude Bernard-Lyon 1 and Ecole Supérieure de Chimie Physique et Electronique de Lyon, Villeurbanne, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't