Structural analysis of the multienzyme aminoacyl‐tRNA synthetase complex: A three‐domain model based on reversible chemical crosslinking
Abstract
A subset of eukaryotic aminoacyl‐tRNA synthetases (a‐RS) are contained in a multienzyme complex for which little structural detail is known. Three reversible chemical crosslinking reagents have been used to investigate the arrangement of polypeptides within this particle as isolated from rabbit reticulocytes. Identification of the crosslinked protein pairs was accomplished by two‐dimensional SDS diagonal gel electrophoresis. Seventeen neighboring protein pairs have been identified. Eight are seen with at least two reagents: K‐RS:p38, D‐RS:K‐RS, R‐RS dimer, K‐RS dimer, K‐RS:Q‐RS, E/P‐RS:K‐RS, E/P‐RS:I‐RS, and Q‐RS with one of the nonsynthetase proteins. Nine more are observed with one reagent: D‐RS dimer, R‐RS:p43, D‐RS:Q‐RS, D‐RS:M‐RS, K‐RS:L‐RS, I‐RS:R‐RS, D‐RS:E/P‐RS, I‐RS:Q‐RS, I‐RS:L‐RS. One trimeric association is seen: E/P‐RS:I‐RS:L‐RS.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Jan 01, 1998
- Source ID
- 10.1002/pro.5560070108
Entities
People
- J. Anthony Warrington
- Mona T. Norcum
Organizations
- Army Research Office