PMID- 19864422
OWN - NLM
STAT- MEDLINE
DCOM- 20100106
LR  - 20211020
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 284
IP  - 51
DP  - 2009 Dec 18
TI  - Human ISCA1 interacts with IOP1/NARFL and functions in both cytosolic and 
      mitochondrial iron-sulfur protein biogenesis.
PG  - 35297-307
LID - 10.1074/jbc.M109.040014 [doi]
AB  - Iron-sulfur proteins play an essential role in many biologic processes. Hence, 
      understanding their assembly is an important goal. In Escherichia coli, the 
      protein IscA is a product of the isc (iron-sulfur cluster) operon and functions 
      in the iron-sulfur cluster assembly pathway in this organism. IscA is conserved 
      in evolution, but its function in mammalian cells is not known. Here, we provide 
      evidence for a role for a human homologue of IscA, named IscA1, in iron-sulfur 
      protein biogenesis. We observe that small interfering RNA knockdown of IscA1 in 
      HeLa cells leads to decreased activity of two mitochondrial iron-sulfur enzymes, 
      succinate dehydrogenase and mitochondrial aconitase, as well as a cytosolic 
      iron-sulfur enzyme, cytosolic aconitase. IscA1 is observed both in cytosolic and 
      mitochondrial fractions. We find that IscA1 interacts with IOP1 (iron-only 
      hydrogenase-like protein 1)/NARFL (nuclear prelamin A recognition factor-like), a 
      cytosolic protein that plays a role in the cytosolic iron-sulfur protein assembly 
      pathway. We therefore propose that human IscA1 plays an important role in both 
      mitochondrial and cytosolic iron-sulfur cluster biogenesis, and a notable 
      component of the latter is the interaction between IscA1 and IOP1.
FAU - Song, Daisheng
AU  - Song D
AD  - Department of Pathology and Laboratory Medicine, University of Pennsylvania 
      School of Medicine, Philadelphia, Pennsylvania 19104, USA.
FAU - Tu, Zheng
AU  - Tu Z
FAU - Lee, Frank S
AU  - Lee FS
LA  - eng
GR  - R01 GM071459/GM/NIGMS NIH HHS/United States
GR  - R01-GM71459/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CIAO3 protein, human)
RN  - 0 (ISCA1 protein, human)
RN  - 0 (Iron-Sulfur Proteins)
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (RNA, Small Interfering)
RN  - EC 1.12.7.2 (Hydrogenase)
RN  - EC 1.3.99.1 (Succinate Dehydrogenase)
RN  - EC 4.2.1.3 (Aconitate Hydratase)
SB  - IM
MH  - Aconitate Hydratase/*biosynthesis/genetics
MH  - Animals
MH  - COS Cells
MH  - Chlorocebus aethiops
MH  - Cytosol/*metabolism
MH  - Gene Knockdown Techniques
MH  - HeLa Cells
MH  - Humans
MH  - Hydrogenase/genetics/*metabolism
MH  - Iron-Sulfur Proteins/antagonists & inhibitors/genetics/*metabolism
MH  - Mitochondria/*metabolism
MH  - Mitochondrial Proteins/antagonists & inhibitors/*biosynthesis/genetics/metabolism
MH  - Protein Binding/physiology
MH  - RNA, Small Interfering
MH  - Succinate Dehydrogenase/*biosynthesis/genetics
PMC - PMC2790959
EDAT- 2009/10/30 06:00
MHDA- 2010/01/07 06:00
PMCR- 2010/12/18
CRDT- 2009/10/30 06:00
PHST- 2009/10/30 06:00 [entrez]
PHST- 2009/10/30 06:00 [pubmed]
PHST- 2010/01/07 06:00 [medline]
PHST- 2010/12/18 00:00 [pmc-release]
AID - S0021-9258(20)37494-9 [pii]
AID - M109.040014 [pii]
AID - 10.1074/jbc.M109.040014 [doi]
PST - ppublish
SO  - J Biol Chem. 2009 Dec 18;284(51):35297-307. doi: 10.1074/jbc.M109.040014.