The relationship between size of a presecretory protein and extent of signal-recognition-particle-mediated arrest of its translation.
Small eukaryotic presecretory proteins, such as preprocecropinA, prepromelittin, and prepropeptideGLa, are transported into mammalian microsomes both with the aid of ribosome and signal recognition particle (SRP) and independently of these ribonucleoprotein particles. Typically, synthetic extensions of these precursor proteins show the phenotype of naturally occurring large presecretory proteins. However, it was shown that small truncated forms of naturally occurring large presecretory proteins are not transport competent or transport competent only in the presence of the two ribonucleoprotein particles. In order to directly address this apparent paradox, we studied the sensitivities of nascent polypeptide chains, related to preprocecropinA and prepromelittin, to SRP-mediated arrest of elongation and compared them with synthetic extensions of various length.
Jung
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C
Institut für Biochemie und Molekulare Zellbologie, Georg-August-Universität Göttingen, Germany.
Zimmermann
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R
D000818:Animals; D005914:Globins / Q000235:genetics / Q000378:metabolism; D007301:Insect Hormones / Q000235:genetics / Q000378:metabolism*; D019476:Insect Proteins; D008555:Melitten / Q000235:genetics / Q000378:metabolism*; D008970:Molecular Weight; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D018271:Signal Recognition Particle / Q000502:physiology*
C059037:CecA2 protein, Bombyx mori; D007301:Insect Hormones; D019476:Insect Proteins; C088254:PGLa prepropeptide; D011498:Protein Precursors; D012333:RNA, Messenger; D018271:Signal Recognition Particle; D008555:Melitten; C016694:prepromelittin; D005914:Globins