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Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1999 Sep 03; Vol. 1446 (3), pp. 365-70. - Publication Year :
- 1999
-
Abstract
- We isolated two proteins, ECP-51 and ECP-54, from human erythrocyte cytosol by affinity chromatography using a peptide of the integral membrane protein stomatin as bait. Partial amino acid sequence information obtained by microsequencing allowed us to clone the respective cDNAs. Analysis of the nucleotide sequences revealed that ECP-51 and ECP-54 are homologous (44.2% amino acid identity) and contain ATP-binding sites. ECP-54 was identified as TIP49/RUVBL1/NMP238, which is a component of a large nuclear protein complex, possibly the RNA polymerase II holoenzyme; ECP-51 is a novel protein. Using the two-hybrid system, we showed that these proteins interact with each other. The interaction of ECP-51 and ECP-54 with the stomatin peptide and the localization to the nucleus and cytoplasm suggest an additional function for these proteins as chaperone components.
- Subjects :
- ATPases Associated with Diverse Cellular Activities
Amino Acid Sequence
Blood Proteins metabolism
Carrier Proteins chemistry
Carrier Proteins isolation & purification
Chromatography, Affinity
Cloning, Molecular
Cytosol metabolism
DNA Primers
Databases as Topic
Humans
Molecular Sequence Data
Polymerase Chain Reaction
Sequence Alignment
Sequence Homology, Amino Acid
Carrier Proteins genetics
DNA Helicases
Erythrocytes metabolism
Membrane Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1446
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 10524211
- Full Text :
- https://doi.org/10.1016/s0167-4781(99)00104-9