Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: immune mapping of the nascent chain
- PMID: 6808502
- PMCID: PMC346363
- DOI: 10.1073/pnas.79.10.3111
Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: immune mapping of the nascent chain
Abstract
The site of the nascent polypeptide chain as it leaves the ribosome has been localized on the "exit domain" of the Escherichia coli ribosome by using IgG antibodies directed against the enzyme beta-galactosidase (EC 3.2.1.23). Thus, a functional site has been mapped on intact 70S ribosomes. The exit site is on the large subunit, approximately 70 A from the interface between subunits and nearly 150 A from the central protuberance, the likely site of peptide transfer. It is adjacent to the region corresponding to the rough endoplasmic membrane binding region of the eukaryotic ribosome but distant from ribosomal components participating in mRNA recognition and polypeptide elongation (i.e., distant from the "translational domain"). These results, together with the protease protection experiments of others, provide evidence that the nascent protein chain probably passes through the ribosome in an unfolded, fully extended conformation.
Similar articles
-
Nascent polypeptide chains exit the ribosome in the same relative position in both eucaryotes and procaryotes.J Cell Biol. 1983 May;96(5):1471-4. doi: 10.1083/jcb.96.5.1471. J Cell Biol. 1983. PMID: 6341381 Free PMC article.
-
Dual effect of chloramphenicol peptides on ribosome inhibition.Amino Acids. 2017 May;49(5):995-1004. doi: 10.1007/s00726-017-2406-5. Epub 2017 Mar 10. Amino Acids. 2017. PMID: 28283906
-
Properties of intraribosomal part of nascent polypeptide.Biochemistry (Mosc). 2010 Dec;75(13):1517-27. doi: 10.1134/s000629791013002x. Biochemistry (Mosc). 2010. PMID: 21417992 Review.
-
Mechanistic Insight into the Reactivation of BCAII Enzyme from Denatured and Molten Globule States by Eukaryotic Ribosomes and Domain V rRNAs.PLoS One. 2016 Apr 21;11(4):e0153928. doi: 10.1371/journal.pone.0153928. eCollection 2016. PLoS One. 2016. PMID: 27099964 Free PMC article.
-
Identification of binding sites on the E. coli ribosome by affinity labeling.Adv Exp Med Biol. 1977;86A:595-609. doi: 10.1007/978-1-4684-3282-4_35. Adv Exp Med Biol. 1977. PMID: 335842 Review.
Cited by
-
Mapping evolution with ribosome structure: intralineage constancy and interlineage variation.Proc Natl Acad Sci U S A. 1982 Oct;79(19):5948-52. doi: 10.1073/pnas.79.19.5948. Proc Natl Acad Sci U S A. 1982. PMID: 6764534 Free PMC article.
-
Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.J Cell Biol. 1986 Dec;103(6 Pt 1):2253-61. doi: 10.1083/jcb.103.6.2253. J Cell Biol. 1986. PMID: 3097028 Free PMC article.
-
Export and sorting of the Escherichia coli outer membrane protein OmpA.J Bioenerg Biomembr. 1990 Jun;22(3):441-9. doi: 10.1007/BF00763176. J Bioenerg Biomembr. 1990. PMID: 2202726 Review.
-
Ribonucleoparticle-independent transport of proteins into mammalian microsomes.J Bioenerg Biomembr. 1990 Dec;22(6):711-23. doi: 10.1007/BF00786927. J Bioenerg Biomembr. 1990. PMID: 2092035 Review.
-
Site-directed cross-linking studies on the E. coli tRNA-ribosome complex: determination of sites labelled with an aromatic azide attached to the variable loop or aminoacyl group of tRNA.Nucleic Acids Res. 1993 Feb 25;21(4):887-96. doi: 10.1093/nar/21.4.887. Nucleic Acids Res. 1993. PMID: 7680805 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources