Untitled

Graifer, D. M.; Карпова, Г. Г.

doi:10.1023/a:1010558506967

Molecular Biology

2001

DOI: 10.1023/a:1010558506967

|View full text |Cite

Untitled

D. M. Graifer

Г. Г. Карпова

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2002

2005

Publication Types

Select...

Article5

Relationship

Self Cite0

Independent5

Authors

Journals

Cited by 7 publications

(1 citation statement)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Crystals of eukaryotic ribosomal subunits suitable for X-ray analyses still remain unavailable. One of methods applicable to study the positioning of mRNA on both pro- and eukaryotic (including mammalian) ribosomes is site-directed cross-linking ( − ). To date, the nature of the contacts between the components of the A, P, and E sites of human ribosome has been determined using short mRNA analogues, that is, derivatized oligonucleotides in which the nature and site of attachment of the (photo)reactive probe were varied ( − ).…”

mentioning

confidence: 99%

The First Position of a Codon Placed in the A Site of the Human 80S Ribosome Contacts Nucleotide C1696 of the 18S rRNA as Well as Proteins S2, S3, S3a, S30, and S15

et al. 2005

View full text Add to dashboard Cite

Messenger RNA analogues (42-mers) containing a GAC codon (aspartic acid) in the middle of their sequence followed by a s(4)UGA stop codon were used to identify the components of the human ribosomal A site in direct contact with the photoactivatable 4-thiouridine (s(4)U) residue. We compared the behavior of the nonphased ribosome-mRNA complex, (-)tRNA(Asp), to the one of the phased complex, (+)tRNA(Asp), in the absence and in the presence of eRF1, the eukaryotic class 1 translation termination factor of human origin. The patterns of cross-links obtained for the three complexes were similar to those previously reported for rabbit ribosomes [Chavatte, L., et al. (2001) Eur. J. Biochem. 268, 2896-2904]. Cross-links involving proteins S2, S3, S3a, and S30 were poorly dependent on the presence of tRNA(Asp) and eRF1. Cross-linking to nucleotide C1696 of 18S rRNA occurred in all complexes, but its yield was at least two times higher in the phased complex with an empty A site than in the nonphased complex or when the A site was occupied by eRF1. In contrast, protein S15 cross-linked only in the phased complex in the absence of eRF1. The data obtained point to notable differences in organization of the decoding site between mammalian and prokaryotic ribosomes and to large internal mobility of the components of the tRNA (eRF1)-free A site.

show abstract

mentioning

confidence: 99%

The First Position of a Codon Placed in the A Site of the Human 80S Ribosome Contacts Nucleotide C1696 of the 18S rRNA as Well as Proteins S2, S3, S3a, S30, and S15

et al. 2005

View full text Add to dashboard Cite

show abstract

Arrangement of the Template 3′ of the A-Site Codon on the Human 80S Ribosome

et al. 2005

View full text Add to dashboard Cite

Positioning of the mRNA stop signal with respect to polypeptide chain release factors and ribosomal proteins in 80S ribosomes

et al. 2002

View full text Add to dashboard Cite

To study positioning of the mRNA stop signal with respect to polypeptide chain release factors (RFs) and ribosomal components within human 80S ribosomes, photoreactive mRNA analogs were applied. Derivatives of the UUCUAAA heptaribonucleotide containing the UUC codon for Phe and the stop signal UAAA, which bore a perfluoroaryl azido group at either the fourth nucleotide or the 3P P-terminal phosphate, were synthesized. The UUC codon was directed to the ribosomal P site by the cognate tRNA Phe , targeting the UAA stop codon to the A site. Mild UV irradiation of the ternary complexes consisting of the 80S ribosome, the mRNA analog and tRNA resulted in tRNA-dependent crosslinking of the mRNA analogs to the 40S ribosomal proteins and the 18S rRNA. mRNA analogs with the photoreactive group at the fourth uridine (the first base of the stop codon) crosslinked mainly to protein S15 (and much less to S2). For the 3P P-modified mRNA analog, the major crosslinking target was protein S2, while protein S15 was much less crosslinked. Crosslinking of eukaryotic (e) RF1 was entirely dependent on the presence of a stop signal in the mRNA analog. eRF3 in the presence of eRF1 did not crosslink, but decreased the yield of eRF1 crosslinking. We conclude that (i) proteins S15 and S2 of the 40S ribosomal subunit are located near the A site-bound codon; (ii) eRF1 can induce spatial rearrangement of the 80S ribosome leading to movement of protein L4 of the 60S ribosomal subunit closer to the codon located at the A site; (iii) within the 80S ribosome, eRF3 in the presence of eRF1 does not contact the stop codon at the A site and is probably located mostly (if not entirely) on the 60S subunit. ß

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Untitled

Cited by 7 publications

References 25 publications

The First Position of a Codon Placed in the A Site of the Human 80S Ribosome Contacts Nucleotide C1696 of the 18S rRNA as Well as Proteins S2, S3, S3a, S30, and S15

The First Position of a Codon Placed in the A Site of the Human 80S Ribosome Contacts Nucleotide C1696 of the 18S rRNA as Well as Proteins S2, S3, S3a, S30, and S15

Arrangement of the Template 3′ of the A-Site Codon on the Human 80S Ribosome

Positioning of the mRNA stop signal with respect to polypeptide chain release factors and ribosomal proteins in 80S ribosomes

Contact Info

Product

Resources

About