PMID- 10218584
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20220224
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 447
IP  - 1
DP  - 1999 Mar 19
TI  - Human members of the SCO1 gene family: complementation analysis in yeast and
      intracellular localization.
PG  - 65-70
AB  - Cytochrome c oxidase is a multiprotein complex in the mitochondrial membrane
      whose biogenesis requires a number of proteins besides the structural subunits.
      Several yeast proteins as well as a human disease-related protein have been
      reported which are involved in cytochrome c oxidase assembly. The S. cerevisiae
      Sco1p protein has been implicated in the transfer of copper to cytochrome c
      oxidase subunits Cox1p and/or Cox2p. Here we report on the complementation
      behavior in yeast of two recently identified ScSco1p homologs of chromosome 17
      and chromosome 22 from human. When allotropically expressed in yeast, both genes 
      fail to complement the lack of the ScSCO1 gene. However, a chimera of the
      N-terminal half of ScSco1p and the C-terminal half of the chromosome 17 homolog
      does substitute for the ScSco1p function. Interestingly, the respective chimera
      with the human homolog of chromosome 22 is not able to complement. Expression of 
      EGFP fusions in HeLa cells shows that both human ScSco1p homologs are located in 
      the mitochondria of human cells.
FAU - Paret, C
AU  - Paret C
AD  - Institut fur Genetik, Technische Universitat Dresden, Germany.
FAU - Ostermann, K
AU  - Ostermann K
FAU - Krause-Buchholz, U
AU  - Krause-Buchholz U
FAU - Rentzsch, A
AU  - Rentzsch A
FAU - Rodel, G
AU  - Rodel G
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Luminescent Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SCO1 protein, S cerevisiae)
RN  - 0 (SCO1 protein, human)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cell Compartmentation
MH  - Electron Transport Complex IV/biosynthesis
MH  - Genetic Complementation Test
MH  - Green Fluorescent Proteins
MH  - HeLa Cells
MH  - Humans
MH  - Luminescent Proteins/genetics/isolation & purification
MH  - Membrane Proteins/genetics/*isolation & purification/*metabolism
MH  - Microscopy, Fluorescence
MH  - Mitochondria/*chemistry
MH  - Mitochondrial Proteins
MH  - Molecular Chaperones
MH  - Molecular Sequence Data
MH  - Oxygen Consumption
MH  - Recombinant Fusion Proteins/isolation & purification/metabolism
MH  - Saccharomyces cerevisiae/genetics
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
MH  - Species Specificity
EDAT- 1999/04/28 00:00
MHDA- 1999/04/28 00:01
CRDT- 1999/04/28 00:00
PHST- 1999/04/28 00:00 [pubmed]
PHST- 1999/04/28 00:01 [medline]
PHST- 1999/04/28 00:00 [entrez]
AID - S0014-5793(99)00266-5 [pii]
AID - 10.1016/s0014-5793(99)00266-5 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Mar 19;447(1):65-70. doi: 10.1016/s0014-5793(99)00266-5.