PMID- 18270200
OWN - NLM
STAT- MEDLINE
DCOM- 20080522
LR  - 20211020
IS  - 0021-9258 (Print)
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Linking)
VI  - 283
IP  - 14
DP  - 2008 Apr 4
TI  - A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis.
PG  - 9231-8
LID - 10.1074/jbc.M708077200 [doi]
AB  - The biogenesis of cytosolic iron-sulfur (Fe-S) proteins in mammalian cells is 
      poorly understood. In Saccharomyces cerevisiae, there is a pathway dedicated to 
      cytosolic Fe-S protein maturation that involves several essential proteins. One 
      of these is Nar1, which intriguingly is homologous to iron-only hydrogenases, 
      ancient enzymes that catalyze the formation of hydrogen gas in anaerobic 
      bacteria. There are two orthologues of Nar1 in mammalian cells, iron-only 
      hydrogenase-like protein 1 (IOP1) and IOP2 (also known as nuclear prelamin A 
      recognition factor). We examined IOP1 for a potential role in mammalian cytosolic 
      Fe-S protein biogenesis. We found that knockdown of IOP1 in both HeLa and Hep3B 
      cells decreases the activity of cytosolic aconitase, an Fe-S protein, but not 
      that of mitochondrial aconitase. Knockdown of IOP2, in contrast, had no effect on 
      either. The decrease in aconitase activity upon IOP1 knockdown is rescued by 
      expression of a small interference RNA-resistant version of IOP1. Upon loss of 
      its Fe-S cluster, cytosolic aconitase is known to be converted to iron regulatory 
      protein 1, and consistent with this, we found that IOP1 knockdown increases 
      transferrin receptor 1 mRNA levels and decreases ferritin heavy chain protein 
      levels. IOP1 knockdown also leads to a decrease in activity of xanthine oxidase, 
      a distinct cytosolic Fe-S protein. Taken together, these results provide evidence 
      that IOP1 is involved in mammalian cytosolic Fe-S protein maturation.
FAU - Song, Daisheng
AU  - Song D
AD  - Department of Pathology and Laboratory Medicine, University of Pennsylvania 
      School of Medicine, 422 Curie Boulevard, Philadelphia, PA 19104, USA.
FAU - Lee, Frank S
AU  - Lee FS
LA  - eng
GR  - R01 GM071459/GM/NIGMS NIH HHS/United States
GR  - R01 GM 71459/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20080212
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CIAO3 protein, human)
RN  - 0 (Iron-Sulfur Proteins)
RN  - 0 (Metalloproteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Receptors, Transferrin)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 70FD1KFU70 (Sulfur)
RN  - 9013-31-4 (Apoferritins)
RN  - E1UOL152H7 (Iron)
RN  - EC 1.12.7.2 (Hydrogenase)
RN  - EC 1.12.7.2 (Nar1 protein, S cerevisiae)
RN  - EC 1.17.3.2 (Xanthine Oxidase)
RN  - EC 4.2.1.3 (Aconitate Hydratase)
RN  - EC 4.2.1.3 (Iron Regulatory Protein 1)
SB  - IM
MH  - Aconitate Hydratase/biosynthesis/genetics
MH  - Apoferritins/biosynthesis/genetics
MH  - Bacteria, Anaerobic/genetics/metabolism
MH  - Cytosol/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Hydrogenase/genetics/*metabolism
MH  - Iron/metabolism
MH  - Iron Regulatory Protein 1/biosynthesis/genetics
MH  - Iron-Sulfur Proteins/genetics/metabolism
MH  - Metalloproteins/*biosynthesis/genetics
MH  - Mitochondria/genetics/metabolism
MH  - Protein Biosynthesis/*physiology
MH  - RNA Interference
MH  - RNA, Messenger/biosynthesis/genetics
MH  - Receptors, Transferrin/biosynthesis/genetics
MH  - Saccharomyces cerevisiae/genetics/metabolism
MH  - Saccharomyces cerevisiae Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Sulfur/metabolism
MH  - Xanthine Oxidase/biosynthesis/genetics
PMC - PMC2431034
EDAT- 2008/02/14 09:00
MHDA- 2008/05/23 09:00
PMCR- 2009/04/04
CRDT- 2008/02/14 09:00
PHST- 2008/02/14 09:00 [pubmed]
PHST- 2008/05/23 09:00 [medline]
PHST- 2008/02/14 09:00 [entrez]
PHST- 2009/04/04 00:00 [pmc-release]
AID - S0021-9258(20)52889-5 [pii]
AID - 9231 [pii]
AID - 10.1074/jbc.M708077200 [doi]
PST - ppublish
SO  - J Biol Chem. 2008 Apr 4;283(14):9231-8. doi: 10.1074/jbc.M708077200. Epub 2008 
      Feb 12.