Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage

Article Abstract:

Crystal structure analysis of the RNA polymerase II and the transcription elongation factor TFIIS complex reveals that TFIIS extends to the polymerase active site and two acidic amino acid residues in a TFIIS loop complement the RNA polymerase active site enabling it to cleave mRNA by positioning metal ion and water molecule. Data also indicate that TFIIS induces extensive structural changes in the enzyme.

Author: Kettenberger, Hubert, Armache, Karim-Jean, Cramer, Patrick
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
Germany, Messenger RNA, Scission (Chemistry)

User Contributions:

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

CAPTCHA


Structural basis of core promoter recognition in a primitive eukaryote

Article Abstract:

The crystal structures of the apo-initiator binding domain and initiator binding domain-initiator complexes and the c-terminal domain of the initiator binding protein 39 show winged-helix motif and a scaffold similar to ETS-family proteins for initiator binding domains. Data point out that binding of initiator binding protein 39 to the initiator recruits RNA polymerase II and initiates transcription.

Author: Schumacher, Maria A., Lau, Audrey O.T., Johnson, Patricia J.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
Genetic aspects, Eukaryotes, Promoters (Genetics)

User Contributions:

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

CAPTCHA


Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase

Article Abstract:

Crystal structure analysis of the Escherichia coli core RNA polymerase bound to the transcription elongation factor GreB indicates that the GreB N-terminal coiled-coil domian extends to the enzyme active site. Data suggest that conserved acidic amino acid residues at the tip of the Gre factor modify RNA polymerse active site leading to catalysis of cleavage activity by the enzyme.

Author: Opalka, Natacha, Chlenov, Mark, Chacon, Pablo, Rice, William J., Wriggers, Willy, Darst, Seth A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
Escherichia coli, Structure-activity relationships (Biochemistry), Catalysis

User Contributions:

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

CAPTCHA


Subjects list: Analysis, Physiological aspects, Genetic transcription, Transcription (Genetics), RNA polymerases, Binding sites (Biochemistry), Active sites (Biochemistry), Structure, Research, United States
Similar abstracts:
  • Abstracts: Ancient origin of the tryptophan operon and the dynamics of evolutionary change. Leucine biosynthesis in fungi: entering metabolism through the back door
  • Abstracts: S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
  • Abstracts: Gene structure and transcriptional organization of the dnaK operon of Bifidobacterium breve UCC 2003 and application of the operon in Bifidobacterial tracing
  • Abstracts: Inheriting the golgi. Endocytosis by random initiation and stabilization of clathrin-coated pits. Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi
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.