PMID- 10092594
OWN - NLM
STAT- MEDLINE
DCOM- 19990427
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 14
DP  - 1999 Apr 2
TI  - Identification of peroxisomal acyl-CoA thioesterases in yeast and humans.
PG  - 9216-23
AB  - A computer-based screen of the Saccharomyces cerevisiae genome identified YJR019C
      as a candidate oleate-induced gene. YJR019C mRNA levels were increased
      significantly during growth on fatty acids, suggesting that it may play a role in
      fatty acid metabolism. The YJR019C product is highly similar to tesB, a bacterial
      acyl-CoA thioesterase, and carries a tripeptide sequence,
      alanine-lysine-phenylalanineCOOH, that closely resembles the consensus sequence
      for type-1 peroxisomal targeting signals. YJR019C directed green fluorescence
      protein to peroxisomes, and biochemical studies revealed that YJR019C is an
      abundant component of purified yeast peroxisomes. Disruption of the YJR019C gene 
      caused a significant decrease in total cellular thioesterase activity, and
      recombinant YJR019C was found to exhibit intrinsic acyl-CoA thioesterase activity
      of 6 units/mg. YJR019C also shared significant sequence similarity with hTE, a
      human thioesterase that was previously identified because of its interaction with
      human immunodeficiency virus-Nef in the yeast two-hybrid assay. We report here
      that hTE is also a peroxisomal protein, demonstrating that thioesterase activity 
      is a conserved feature of peroxisomes. We propose that YJR019C and hTE be renamed
      as yeast and human PTE1 to reflect the fact that they encode peroxisomal
      thioesterases. The physical segregation of yeast and human PTE1 from the
      cytosolic fatty acid synthase suggests that these enzymes are unlikely to play a 
      role in formation of fatty acids. Instead, the observation that PTE1 contributes 
      to growth on fatty acids implicates this thioesterase in fatty acid oxidation.
FAU - Jones, J M
AU  - Jones JM
AD  - Department of Biological Chemistry, The Johns Hopkins University School of
      Medicine, Baltimore, Maryland 21205, USA.
FAU - Nau, K
AU  - Nau K
FAU - Geraghty, M T
AU  - Geraghty MT
FAU - Erdmann, R
AU  - Erdmann R
FAU - Gould, S J
AU  - Gould SJ
LA  - eng
SI  - GENBANK/AF124264
SI  - GENBANK/AF124265
GR  - DK45787/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Fungal)
RN  - 0 (Luminescent Proteins)
RN  - 0 (RNA, Messenger)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - 2UMI9U37CP (Oleic Acid)
RN  - EC 3.1.2.- (Thiolester Hydrolases)
RN  - EC 3.1.2.2 (ACOT8 protein, human)
RN  - EC 3.1.2.2 (Palmitoyl-CoA Hydrolase)
SB  - IM
SB  - X
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Consensus Sequence
MH  - DNA, Fungal/chemistry
MH  - Fluorescent Antibody Technique, Indirect
MH  - Gene Expression Regulation, Enzymologic/drug effects
MH  - Green Fluorescent Proteins
MH  - Humans
MH  - Luminescent Proteins/genetics
MH  - Microbodies/*enzymology
MH  - Microscopy, Fluorescence
MH  - Molecular Sequence Data
MH  - Oleic Acid/pharmacology
MH  - Open Reading Frames
MH  - Palmitoyl-CoA Hydrolase/genetics/metabolism
MH  - RNA, Messenger/metabolism
MH  - Saccharomyces cerevisiae/*enzymology/genetics
MH  - Sequence Alignment
MH  - Thiolester Hydrolases/*genetics/*metabolism
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
AID - 10.1074/jbc.274.14.9216 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 2;274(14):9216-23. doi: 10.1074/jbc.274.14.9216.