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J. Biol. Chem., Vol. 263, Issue 20, 9646-9650, 07, 1988
N Campos, J Palau, M Torrent and D Ludevid
We show that maize storage protein translocation across microsomal
membranes is mediated by signal recognition particles (SRPs) similar to
those described in animal systems (Dobberstein, B. (1978) Hoppe- Seyler's
Z. Physiol. Chem. 252, 955-962; Walter, P., and Blobel, G. (1980) Proc.
Natl. Acad. Sci. U. S. A. 77, 7112-7116). We have prepared a high salt
extract from endosperm cell homogenates, from which a ribosome-free
fraction was obtained. This fraction is enriched in an SRP-like factor
which apparently corresponds to a ribonucleoprotein particle that sediments
at about 12 S. The RNA moiety of this 12 S particle is complex, showing a
three-band electrophoretic pattern and sedimenting at about 8 S. The
fraction restores translocation competence of salt-washed maize microsomes
as tested by using a pre- zein message. In contrast to canine SRPs, the
maize SRP-like component does not cause a translation arrest of maize
storage proteins (zein) in a wheat germ cell-free system.
Signal recognition-like particles are present in maize
Departamento de Biologia Molecular i Agrobiologia, Centre d'Investigacio i Desenvolupament Consejo Superior de Investigacions Cientificas, Jordi Girona Salgado, Barcelona, Spain.
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