PUBLICATION
Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution
- Authors
- Wakasugi, K., and Morishima, I.
- ID
- ZDB-PUB-050404-1
- Date
- 2005
- Source
- Biochemical and Biophysical Research Communications 330(2): 591-597 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Circular Dichroism
- DNA Primers
- Electrophoresis, Polyacrylamide Gel
- Globins/chemistry*
- Humans
- Molecular Sequence Data
- Nerve Tissue Proteins/chemistry*
- Nuclear Magnetic Resonance, Biomolecular
- Protein Denaturation
- Recombinant Fusion Proteins/chemistry*
- Sequence Homology, Amino Acid
- Zebrafish
- PubMed
- 15796924 Full text @ Biochem. Biophys. Res. Commun.
Citation
Wakasugi, K., and Morishima, I. (2005) Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution. Biochemical and Biophysical Research Communications. 330(2):591-597.
Abstract
Neuroglobin (Ngb) is a recently discovered vertebrate heme protein that can reversibly bind oxygen that is expressed in the brain. Zebrafish and human Ngb share about 50% amino acid sequence identity. These Ngb proteins consist of four compact protein structural unit "modules" referred to as M1-M4. In the present study, we investigated the effects of module substitution on the properties of Ngb. Specifically, we prepared and characterized a chimeric ZHZZ Ngb in which the heme-binding module M2 of zebrafish Ngb was replaced by the comparable human Ngb module. Our results showed that the chimeric ZHZZ was stable and formed almost the identical heme-environmental and alpha-helical structure as the human and zebrafish Ngb proteins, suggesting that the structure of Ngb has been evolutionarily conserved.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping