PMID- 10488108
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 39
DP  - 1999 Sep 24
TI  - The RING finger motif of photomorphogenic repressor COP1 specifically interacts 
      with the RING-H2 motif of a novel Arabidopsis protein.
PG  - 27674-81
AB  - The constitutive photomorphogenic 1 (COP1) protein of Arabidopsis functions as a 
      molecular switch for the seedling developmental fates: photomorphogenesis under 
      light conditions and skotomorphogenesis in darkness. The COP1 protein contains a 
      cysteine-rich zinc-binding RING finger motif found in diverse groups of 
      regulatory proteins. To understand the role of the COP1 RING finger in mediating 
      protein-protein interaction, we have performed a yeast two-hybrid screen and 
      isolated a novel protein with a RING-H2 motif, a variant type of the RING finger. 
      This protein, designated COP1 Interacting Protein 8 (CIP8), is encoded by a 
      single copy gene and localized to cytosol in a transient assay. In addition to 
      the RING-H2 motif, the predicted protein has a C4 zinc finger, an acidic region, 
      a glycine-rich cluster, and a serine-rich cluster. The COP1 RING finger and the 
      CIP8 RING-H2 domains are sufficient for their interaction with each other both in 
      vitro and in yeast, whereas neither motif displayed significant self-association. 
      Moreover, site-directed mutagenesis studies demonstrated that the expected 
      zinc-binding ligands of the RING finger and RING-H2 fingers are essential for 
      their interaction. Our findings indicate that the RING finger motif, in this 
      case, serves as autonomous protein-protein interaction domain. The allele 
      specific effect of cop1 mutations on the CIP8 protein accumulation in seedlings 
      indicates that its stability in vivo is dependent on the COP1 protein.
FAU - Torii, K U
AU  - Torii KU
AD  - Department of Molecular, Cellular, and Developmental Biology, Yale University, 
      New Haven, Connecticut 06520-8104, USA.
FAU - Stoop-Myer, C D
AU  - Stoop-Myer CD
FAU - Okamoto, H
AU  - Okamoto H
FAU - Coleman, J E
AU  - Coleman JE
FAU - Matsui, M
AU  - Matsui M
FAU - Deng, X W
AU  - Deng XW
LA  - eng
SI  - GENBANK/AF162150
GR  - DK09070/DK/NIDDK NIH HHS/United States
GR  - GM47850/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
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 (Arabidopsis Proteins)
RN  - 0 (CIP8 protein, Arabidopsis)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (Plant Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Repressor Proteins)
RN  - EC 2.3.2.27 (AT2G32950 protein, Arabidopsis)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arabidopsis/genetics/*growth & development/*metabolism
MH  - *Arabidopsis Proteins
MH  - Base Sequence
MH  - Carrier Proteins/*chemistry/genetics/*metabolism
MH  - Cytosol/metabolism
MH  - DNA Primers
MH  - Light
MH  - Molecular Sequence Data
MH  - Morphogenesis
MH  - Mutagenesis, Site-Directed
MH  - Plant Proteins/*chemistry/genetics/*metabolism
MH  - Polymerase Chain Reaction
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Repressor Proteins/chemistry/*metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - *Ubiquitin-Protein Ligases
EDAT- 1999/09/17 00:00
MHDA- 1999/09/17 00:01
CRDT- 1999/09/17 00:00
PHST- 1999/09/17 00:00 [pubmed]
PHST- 1999/09/17 00:01 [medline]
PHST- 1999/09/17 00:00 [entrez]
AID - S0021-9258(19)52171-8 [pii]
AID - 10.1074/jbc.274.39.27674 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 24;274(39):27674-81. doi: 10.1074/jbc.274.39.27674.