PMID- 10051604
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 5
DP  - 1999 Mar 2
TI  - Human PEX19: cDNA cloning by functional complementation, mutation analysis in a
      patient with Zellweger syndrome, and potential role in peroxisomal membrane
      assembly.
PG  - 2116-21
AB  - At least 11 complementation groups (CGs) have been identified for the peroxisome 
      biogenesis disorders (PBDs) such as Zellweger syndrome, for which seven
      pathogenic genes have been elucidated. We have isolated a human PEX19 cDNA
      (HsPEX19) by functional complementation of peroxisome deficiency of a mutant
      Chinese hamster ovary cell line, ZP119, defective in import of both matrix and
      membrane proteins. This cDNA encodes a hydrophilic protein (Pex19p) comprising
      299 amino acids, with a prenylation motif, CAAX box, at the C terminus.
      Farnesylated Pex19p is partly, if not all, anchored in the peroxisomal membrane, 
      exposing its N-terminal part to the cytosol. A stable transformant of ZP119 with 
      HsPEX19 was morphologically and biochemically restored for peroxisome biogenesis.
      HsPEX19 expression also restored peroxisomal protein import in fibroblasts from a
      patient (PBDJ-01) with Zellweger syndrome of CG-J. This patient (PBDJ-01)
      possessed a homozygous, inactivating mutation: a 1-base insertion, A764, in a
      codon for Met255, resulted in a frameshift, inducing a 24-aa sequence entirely
      distinct from normal Pex19p. These results demonstrate that PEX19 is the
      causative gene for CG-J PBD and suggest that the C-terminal part, including the
      CAAX homology box, is required for the biological function of Pex19p. Moreover,
      Pex19p is apparently involved at the initial stage in peroxisome membrane
      assembly, before the import of matrix protein.
FAU - Matsuzono, Y
AU  - Matsuzono Y
AD  - Department of Biology, Faculty of Science, Kyushu University, Fukuoka 812-8581,
      Japan.
FAU - Kinoshita, N
AU  - Kinoshita N
FAU - Tamura, S
AU  - Tamura S
FAU - Shimozawa, N
AU  - Shimozawa N
FAU - Hamasaki, M
AU  - Hamasaki M
FAU - Ghaedi, K
AU  - Ghaedi K
FAU - Wanders, R J
AU  - Wanders RJ
FAU - Suzuki, Y
AU  - Suzuki Y
FAU - Kondo, N
AU  - Kondo N
FAU - Fujiki, Y
AU  - Fujiki Y
LA  - eng
SI  - GENBANK/AB018541
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Proteins)
RN  - 0 (PEX19 protein, S cerevisiae)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CHO Cells
MH  - Clone Cells
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - DNA Mutational Analysis
MH  - DNA Primers
MH  - DNA, Complementary
MH  - Gene Library
MH  - Genetic Complementation Test
MH  - Humans
MH  - Intracellular Membranes/chemistry/metabolism
MH  - Liver/metabolism
MH  - Mammals
MH  - Membrane Proteins/chemistry/*genetics/metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Saccharomyces cerevisiae/genetics
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Zellweger Syndrome/*genetics
PMC - PMC26746
EDAT- 1999/03/03 00:00
MHDA- 1999/03/03 00:01
CRDT- 1999/03/03 00:00
PHST- 1999/03/03 00:00 [pubmed]
PHST- 1999/03/03 00:01 [medline]
PHST- 1999/03/03 00:00 [entrez]
AID - 10.1073/pnas.96.5.2116 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2116-21. doi: 10.1073/pnas.96.5.2116.