A Novel Human Striated Muscle RING Zinc Finger Protein, SMRZ, Interacts with SMT3b via Its RING Domain

The RING domain is a conserved zinc finger motif, which serves as a protein-protein interaction interface. Searches of a human heart expressed sequence tag data base for genes encoding the RING domain identified a novel cDNA, named striated muscle RING zinc finger protein (SMRZ). The SMRZ cDNA is 1....

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2001-06, Vol.276 (26), p.23992-23999
Main Authors: Dai, Ken-Shwo, Liew, Choong-Chin
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Nucleus - metabolism
Chromosome 1
Chromosomes, Human, Pair 1
Cloning, Molecular
Humans
Ligases
Molecular Sequence Data
Muscle Proteins
Muscle, Skeletal - metabolism
Mutagenesis, Site-Directed
Protein Structure, Tertiary
RNA, Messenger - biosynthesis
Sequence Homology, Amino Acid
Small Ubiquitin-Related Modifier Proteins
SMRZ protein
SMT3b protein
Tissue Distribution
Tripartite Motif Proteins
Two-Hybrid System Techniques
Ubiquitin-Protein Ligases
Ubiquitins - metabolism
zinc finger
Zinc Fingers
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The RING domain is a conserved zinc finger motif, which serves as a protein-protein interaction interface. Searches of a human heart expressed sequence tag data base for genes encoding the RING domain identified a novel cDNA, named striated muscle RING zinc finger protein (SMRZ). The SMRZ cDNA is 1.9 kilobase pairs in length and encodes a polypeptide of 288 amino acid residues; analysis of the peptide sequence demonstrated an N-terminal RING domain. Fluorescence in situ hybridization localized SMRZ to chromosome 1p33–34. Northern blots demonstrated that SMRZ is expressed exclusively in striated muscle. In the cardiovascular system, SMRZ is more highly expressed in the fetal heart than in the adult heart (slightly higher expression in the ventricle than in the atrium), suggesting that SMRZ is developmentally regulated. SMRZ was found to interact with SMT3b, a ubiquitin-like protein, through the SMRZ-RING domain. This interaction was abolished by mutagenesis of conserved RING domain residues. Transient transfection of SMRZ into C2C12 myoblasts showed localization of SMRZ to the nucleus. These data suggest that SMRZ may play an important role in striated muscle cell embryonic development and perhaps in cell cycle regulation.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M011208200