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(Received for publication, June 24, 1996, and in revised form, August 1, 1996)
From the Most peroxisomal matrix proteins contain a
carboxyl-terminal tripeptide that directs them to peroxisomes. Within
limits, these amino acids may be varied, without loss of function. The
specificity of this peroxisomal targeting signal (PTS1) is remarkable
considering its small size and its relaxed consensus sequence.
Moreover, several peroxisomal proteins have a PTS1-like signal that
does not fit the reported consensus sequence. Because many of these
PTS1 variants seem to be functional in a species-dependent
or protein context-dependent manner, we investigated the
PTS1 requirements in a homologous context, using Saccharomyces
cerevisiae and endogenous peroxisomal malate dehydrogenase
(MDH3). Peroxisomal import of the MDH3-PTS1 variants was tested
qualitatively by the ability to complement the
Volume 271, Number 42,
Issue of October 18, 1996
pp. 26375-26382
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
and
Department of Biochemistry, Academic Medical
Centre, Meibergdreef 15, 1105 AZ, Amsterdam, The Netherlands, the
Departments of Pediatrics and Clinical Biochemistry, Academic
Medical Centre, Meibergdreef 9, 1105 AZ, Amsterdam, The Netherlands,
and the '' Department of Cell Biology, Utrecht University School of
Medicine, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands
mdh3
mutant and quantitatively by subcellular fractionation. We observed
efficient import of MDH3 into peroxisomes with a large variety of PTS1
tripeptides. Many of these variants do not fit the observed PTS1
requirements for heterologously expressed proteins, which suggests that
additional domains in the protein may be of decisive importance whether
or not a certain PTS1 variant is recognized by the components of the
peroxisomal import machinery. Because we show that dimerization of MDH3
precedes import into the organelle, these domains are most likely
conformational domains.
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