sh.sePublications
Change search
ReferencesLink to record
Permanent link

Direct link
Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase
Show others and affiliations
2001 (English)In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 27, no 5, 427-438 p.Article in journal (Refereed) Published
Abstract [en]

Determinants for the recognition of a mitochondrial presequence by the mitochondrial processing peptidase (MPP) have been investigated using mutagenesis and bioinformatics approaches. All plant mitochondrial presequences with a cleavage site that was confirmed by experimental studies can be grouped into three classes. Two major classes contain an arginine residue at position -2 or -3, and the third class does not have any conserved arginines. Sequence logos revealed loosely conserved cleavage motifs for the first two classes but no significant amino acid conservation for the third class. Investigation of processing determinants for a class III precursor, Nicotiana plumbaginifolia F(1)beta precursor of ATP synthase (pF(1)beta), was performed using a series of pF(1)beta presequence mutants and mutant presequence peptides derived from the C-terminal portion of the presequence. Replacement of -2 Gln by Arg inhibited processing, whereas replacement of either the most proximally located -5 Arg or -15 Arg by Leu had only a low inhibitory effect. The C-terminal portion of the pF(1)beta presequence forms a helix-turn-helix structure. Mutations disturbing or prolonging the helical element upstream of the cleavage site inhibited processing significantly. Structural models of potato MPP and the C-terminal pF(1)beta presequence peptide were built by homology modelling and empirical conformational energy search methods, respectively. Molecular docking of the pF(1)beta presequence peptide to the MPP model suggested binding of the peptide to the negatively charged binding cleft formed by the alpha -MPP and beta -MPP subunits in close proximity to the H111XXE114H115X(116-190)E191 proteolytic active site on beta -MPP. Our results show for the first time that the amino acid at the -2 position, even if not an arginine, as well as structural properties of the C-terminal portion of the presequence are important determinants for the processing of a class III precursor by MPP.

Place, publisher, year, edition, pages
2001. Vol. 27, no 5, 427-438 p.
Keyword [en]
mitochondrial processing peptidase, cytochrome bc(1) complex, protein processing, presequence, mitochondrial biogenesis, computer modelling
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:sh:diva-6266ISI: 000171285900006OAI: oai:DiVA.org:sh-6266DiVA: diva2:398718
Available from: 2011-02-18 Created: 2011-02-18 Last updated: 2016-10-07Bibliographically approved

Open Access in DiVA

No full text

Search in DiVA

By author/editor
Sjöling, Sara
In the same journal
The Plant Journal
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

Total: 64 hits
ReferencesLink to record
Permanent link

Direct link