PMID- 10430017
OWN - NLM
STAT- MEDLINE
DCOM- 19990928
LR  - 20190412
IS  - 0171-9335 (Print)
IS  - 0171-9335 (Linking)
VI  - 78
IP  - 6
DP  - 1999 Jun
TI  - Identification and characterization of the human peroxin PEX3.
PG  - 357-74
AB  - The biogenesis of peroxisomes requires the interaction of several peroxins,
      encoded by PEX genes and is well conserved between yeast and humans. We have
      cloned the human cDNA of PEX3 based on its homology to different yeast PEX3
      genes. The deduced peroxin HsPEX3 is a peroxisomal membrane protein with a
      calculated molecular mass of 42.1 kDa. We created N- and C-terminal tagged PEX3
      to assay its topology at the peroxisomal membrane by immunofluorescence
      microscopy. Our results and the one predicted transmembrane spanning region are
      in line with the assumption that H sPEX3 is an integral peroxisomal membrane
      protein with the N-terminus inside the peroxisome and the C-terminus facing the
      cytoplasm. The farnesylated peroxisomal membrane protein PEX19 interacts with
      HsPEX3 in a mammalian two-hybrid assay in human fibroblasts. The physical
      interaction could be confirmed by coimmunoprecipitation of the two in vitro
      transcribed and translated proteins. To address the targeting of PEX3 to the
      peroxisomal membrane, the expression of different N- and C-terminal PEX3
      truncations fused to green fluorescent protein (GFP) was investigated in human
      fibroblasts. The N-terminal 33 amino acids of PEX3 were necessary and sufficient 
      to direct the reporter protein GFP to peroxisomes and seemed to be integrated
      into the peroxisomal membrane. The expression of a 1-16 PEX3-GFP fusion protein
      did not result in a peroxisomal localization, but interestingly, this and several
      other truncated PEX3 fusion proteins were also localized to tubular and/or
      vesicular structures representing mitochondria.
FAU - Soukupova, M
AU  - Soukupova M
AD  - Institut fur Physiologische Chemie, Systembiochemie, Ruhr-Universitat Bochum,
      Germany.
FAU - Sprenger, C
AU  - Sprenger C
FAU - Gorgas, K
AU  - Gorgas K
FAU - Kunau, W H
AU  - Kunau WH
FAU - Dodt, G
AU  - Dodt G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Eur J Cell Biol
JT  - European journal of cell biology
JID - 7906240
RN  - 0 (ATP-Binding Cassette Transporters)
RN  - 0 (Fungal Proteins)
RN  - 0 (Lipoproteins)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (PEX19 protein, S cerevisiae)
RN  - 0 (PEX3 protein, S cerevisiae)
RN  - 0 (Peroxins)
RN  - 0 (Pex3 protein, human)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SPF1 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
SB  - IM
MH  - *ATP-Binding Cassette Transporters
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Cell Compartmentation
MH  - Cell Line
MH  - Fibroblasts/metabolism
MH  - Fungal Proteins/genetics
MH  - Genes, Reporter
MH  - Genetic Complementation Test
MH  - Green Fluorescent Proteins
MH  - Humans
MH  - Intracellular Membranes/metabolism
MH  - Lipoproteins/genetics/*metabolism
MH  - Luminescent Proteins/genetics/metabolism
MH  - Membrane Proteins/genetics/*metabolism
MH  - Mice
MH  - Microbodies/metabolism
MH  - Mitochondria/metabolism
MH  - Molecular Sequence Data
MH  - Peroxins
MH  - Peroxisomal Disorders/metabolism
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Saccharomyces cerevisiae
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
EDAT- 1999/08/03 00:00
MHDA- 1999/08/03 00:01
CRDT- 1999/08/03 00:00
PHST- 1999/08/03 00:00 [pubmed]
PHST- 1999/08/03 00:01 [medline]
PHST- 1999/08/03 00:00 [entrez]
AID - S0171-9335(99)80078-8 [pii]
AID - 10.1016/S0171-9335(99)80078-8 [doi]
PST - ppublish
SO  - Eur J Cell Biol. 1999 Jun;78(6):357-74. doi: 10.1016/S0171-9335(99)80078-8.