The ATP requiring step in assembly of M13 procoat protein into microsomes is related to preservation of transport competence of the precursor protein.
AUTOR(ES)
Wiech, H
RESUMO
M13 procoat protein is processed to transmembrane coat protein by dog pancreas microsomes after completion of synthesis and in the absence of the signal recognition particle (SRP)/docking protein system. ATP is required for fast and efficient processing of procoat protein by microsomes in a reticulocyte lysate. Requirement for ATP is also observed in the absence of ribosomes or docking protein. This indicates the existence of a unique assembly pathway for procoat protein into microsomes which depends on ATP but does not depend on the SRP/docking protein and ribosome/ribosome receptor systems. We suggest that the ATP requirement is linked to a so far unknown component of the reticulocyte lysate, acting on transport competence of precursor proteins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=553497Documentos Relacionados
- The purification of M13 procoat, a membrane protein precursor.
- Mechanisms of membrane assembly: effects of energy poisons on the conversion of soluble M13 coliphage procoat to membrane-bound coat protein.
- Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion.
- Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes.
- Procoat, the precursor of M13 coat protein, inserts post-translationally into the membrane of cells infected by wild-type virus.
