Mutations at the stromal processing peptidase cleavage site of a thylakoid lumen protein precursor affect the rate of processing but not the fidelity.-Reference-Cited by-同舟云学术

Mutations at the stromal processing peptidase cleavage site of a thylakoid lumen protein precursor affect the rate of processing but not the fidelity.

Published:1994-06 Issue:23 Volume:269 Page:16062-16066
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bassham D.C.,Creighton A.M.,Karnauchov I.,Herrmann R.G.,Klösgen R.B.,Robinson C.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. Soluble Chloroplast Enzyme Cleaves preLHCP Made in Escherichia coli to a Mature Form Lacking a Basic N-Terminal Domain

2. Transport of proteins into chloroplasts. Delineation of envelope “transit” and thylakoid “transfer” signals within the pre-sequences of three imported thylakoid lumen proteins.

3. Determinants for cleavage of the chlorophyll a/b binding protein precursor: a requirement for a basic residue that is not universal for chloroplast imported proteins.

4. A conserved cleavage-site motif in chloroplast transit peptides

5. A thylakoid processing protease is required for complete maturation of the lumen protein plastocyanin

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1. Function of the stromal processing peptidase in the chloroplast import pathway;Physiologia Plantarum;2005-04

2. Chloroplast stromal processing peptidase;Handbook of Proteolytic Enzymes;2004

3. Signal Peptidases;Chemical Reviews;2002-11-08

4. Determinants for Removal and Degradation of Transit Peptides of Chloroplast Precursor Proteins;Journal of Biological Chemistry;2002-11

5. Stromal Processing Peptidase Binds Transit Peptides and Initiates Their Atp-Dependent Turnover in Chloroplasts;Journal of Cell Biology;1999-10-04