Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Specific functional interactions of nucleotides at key (super -)3 and (super +)4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex

Article Abstract:

Eukaryotic initiation factor (eIF) 1 maintains the fidelity of initiation codon selection and enables mammalian 48S preinitiation complexes to discriminate against AUG codons, in which the purines at (super -)3 and (super +)4 positions are most important. Results of UV cross-linking experiments and assays of 48S complex formation done indicate that eIF2alpha's interaction with the (super -)3 purine is responsible for recognition of the (super -)3 context position by 48S complexes.

Author: Pestova, Tatyana V., Kolupaeva, Victoria G., Hellen, Christopher U.T., Merrick, William C., Pisarev, Andrey V., Pisareva, Vera P.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2006
United States, Biological Product (except Diagnostic) Manufacturing, Nucleic Acid Derivatives, Nucleotides, Genetic translation, Translation (Genetics), Genetic code

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Position of eukaryotic initiation factor eIFI on the 40S ribosomal subunit determined by directed hydroxyl radical probing

Article Abstract:

The position of eukaryoic initiation factor (e1F1) on the 40S ribosomal subunit is determined using directed hydroxyl radical cleavage to understand the discriminatory role played by e1F1. The position of eIF1 on the 40S subunit suggests that its position close to the P-site is very favorable for an indirect mechanism of eIF1's action.

Author: Pestova, Tatyana V., Kolupaeva, Victoria G., Wagner, Gerhard, Lomakin, Ivan B., Marintchev, Assen
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2003
Cells (Biology), Cells, Hydroxylases, Genetic research

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Structural basis for the enhancement of eIF4A helicase activity by eIF4G

Article Abstract:

The eukaryotic translation initiation factors 4A (eIF4A) and 4G (eIF4G) are crucial for the assembly of the translationally active ribosome. Even though both eIF4A domains play a role in binding the middle domain of eIF4G, the main interaction surface is located on the C-terminal domain.

Author: Wagner, Gerhard, Marintchev, Assen, Oberer, Monika
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2005
Drugs, Cellular Protein, In-Vitro Diagnostic Substance Manufacturing, Eukaryotes, Cellular proteins

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Ribosomes
Similar abstracts:
  • Abstracts: Elimination of Mcl-1 is reguired for the initiation of apoptosis following ultraviolet irradiation. Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis
  • Abstracts: BMAL1-dependent circadian oscillation of nuclear CLOCK: posttranslational events induced by dimerization of trancriptional activators of the mammalian clock system
  • Abstracts: Enigmas of mammalian gamete form and function. 'O sibling, where art thou?' - a review of avian sibling recognition with respect to the mammalian literature
  • Abstracts: Global transcriptional regulation of the locus encoding the skeletal muscle determination genes Mrf4 and Myf5
  • Abstracts: ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Ecsit-ement on the crossroads of Toll and BMP signal transduction
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.