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Thursday, July 23, 2020 | History

3 edition of The heterodimeric elongin BC complex found in the catalog.

The heterodimeric elongin BC complex

Christopher Scott Brower

The heterodimeric elongin BC complex

by Christopher Scott Brower

  • 363 Want to read
  • 37 Currently reading

Published by [s.n.] .
Written in English

    Subjects:
  • Amino Acid Sequence,
  • Ligases,
  • Molecular Sequence Data,
  • Mutagensis, Site-Directed,
  • Protein Binding,
  • RNA Polymerase II,
  • Sequence Alignment,
  • Sequence Homology, Amino Acid,
  • Transcription Factors,
  • Ubiquitin,
  • chemistry,
  • metabolism

  • The Physical Object
    FormatUnknown Binding
    ID Numbers
    Open LibraryOL10344963M
    ISBN 10049318371X
    ISBN 109780493183718
    OCLC/WorldCa47221062

    Elongin C was found to be highly dynamic in the Elongin BC complex while Elongin B was much more stable. Recombinant full length Vif interacted with the Elongin BC complex in vitro with a Kd of µM and resulted in observable changes in deuterium uptake in both Elongin C and B. The elongin BC complex has recently been shown to be a potential target for regulation by the product of the von Hippel–Lindau (VHL) tumor suppressor gene (, ).The VHL gene is mutated in families with VHL disease, a rare genetic disorder (incidence ~ 1 in 36,) that predisposes affected individuals to a variety of cancers, including retinal hemangiomas, central nervous system.

    Ashok N. Hegde, in Learning and Memory: A Comprehensive Reference (Second Edition), Von Hippel-Lindau-Elongin B-Elongin C Complex. The VBC (VHL-elongin B-elongin C) complex was identified in association with the VHL (von Hippel-Lindau) tumor-suppressor structure of this complex is similar to that of the SCF complex. tin ligases include the heterodimeric Elongin BC complex, composed of the Elongin C protein, which is similar in sequence to the Skp1 ubiq-uitin ligase subunit, and Elongin B protein (Figure 1A.

      SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).   Likewise, VHL, the substrate receptor of the VBC ligase complex, is tethered to the hCul2/Rbx1 ligase core through the elongin C protein, which shares structural similarity with Skp1 (Kamura et al., ). The association between VHL and the elongin BC complex is mediated by the SOCS-box motif of VHL (Kamuraet al., ).


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The heterodimeric elongin BC complex by Christopher Scott Brower Download PDF EPUB FB2

The mammalian elongin BC complex is a heterodimer, composed of the amino acid, ubiquitin-like elongin B protein and the amino acid elongin C protein. The elongin BC complex interacts through a short, degenerate BC-box motif with multiple proteins, including the transcription factor elongin A, the von Hippel-Lindau (VHL) tumor suppressor.

The mammalian elongin BC complex is a heterodimer, composed of the amino acid ubiquitin-like elongin B protein and the amino acid elongin C protein. The heterodimeric Elongin BC complex has been shown to interact in vitro and in mammalian cells with a conserved BC-box motif found in a growing number of proteins including RNA polymerase II elongation factor Elongin A, SOCS-box proteins, and the von Hippel-Lindau (VHL) tumor suppressor protein.

Recently, the VHL-Elongin BC complex was found to interact with a module Cited by: The mammalian elongin BC complex is a heterodimer, composed of the amino acid, ubiquitin-like elongin B protein and the amino acid elongin C protein.

Cul2 and Cul5 ubiquitin ligases each include the heterodimeric Elongin BC complex, composed of the amino acid Elongin C protein, which is similar in sequence to the Skp1-Cullin1-F box (SCF) ubiquitin ligase subunit Skp1, and the amino acid Elongin B protein, which includes an N-terminal ubiquitin-like domain and a 34 amino acid C-terminal extension.

The Elongin A–Elongin BC complex assembles with a Cul5/Rbx2 module to reconstitute a ubiquitin ligase of Rpb1 in vitro. (A) Sf9 cells were coinfected with the baculoviruses indicated in the figure. Elongin B is found in cells as a subunit of the heterodimeric Elongin BC complex, which was originally identified as a positive regulator of RNA polymerase II elongation factor Elongin A and subsequently as a component of the multiprotein von Hippel-Lindau tumor suppressor and suppressor of cytokine signaling complexes.

Cul2 and Cul5 ubiquitin ligases each include the heterodimeric Elongin BC complex, composed of the amino acid Elongin C protein, which is similar in sequence to the Skp1-Cullin1-F box ubiquitin ligase subunit Skp1, and the. SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites.

Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed).

The heterodimeric Elongin BC complex has been shown to interact in vitro and in cells with a conserved BC-box motif found in an increasing number of proteins including RNA polymerase II elongation factor Elongin A, suppressor of cytokine signaling (SOCS)-box proteins, and the von Hippel–Lindau tumor suppressor protein.

Recently, the Elongin BC complex was found to function. The heterodimeric Elongin BC complex has been shown to interact in vitro and in mammalian cells with a conserved BC-box motif found in a growing number of proteins including RNA polymerase II elongation factor Elongin A, SOCS-box proteins, and the von Hippel-Lindau (VHL) tumor suppressor protein.

Recently, the. Elongin BC is an abundant cellular complex that interacts with several regulatory proteins in addition to VHL (Kamura et al. ) including the transcription elongation factor elongin A as well as members of the suppressors of cytokine signaling (SOCS) proteins (18, 49).

All of these proteins share a sequence motif called the SOCS box that is. Human Elongin B and C were originally identified as part of the heterotrimeric transcription factor Elongin ABC complex, 1 which promotes elongation during transcription by suppressing pausing of RNA polymerase II.

2 Elongin B and C also have the ability to form the heterodimeric Elongin BC complex, which associates with cellular proteins that. the Elongin BC complex and a heterodimeric module com-posed of a member of the Cullin protein family and RING finger protein Rbx1 or Rbx2 to form multiprotein ubiquitin ligase complexes (Kamura et al,).

In mammalian cells the Cullin protein family includes at least. Elongin B is found in cells as a subunit of the heterodimeric Elongin BC complex, which was originally identified as a positive regulator of RNA polymerase II elongation factor Elongin A and subsequently as a component of the multiprotein von Hippel-Lindau tumor suppressor and suppressor of cytokine signaling complexes.

The heterodimeric Elongin BC complex has been shown to interact in vitro and in cells with a conserved BC-box motif found in an increasing number of proteins including RNA polymerase II elongation factor Elongin A, suppressor of cytokine signaling (SOCS)-box proteins, and the von Hippel-Lindau tumor suppressor protein.

The heterodimeric Elongin BC complex has been shown to interact in vitro and in cells with a conserved BC-box motif found in an increasing number of proteins including RNA polymerase II elon-gation factor Elongin A, suppressor of cytokine signaling (SOCS).

The heterodimeric Elongin BC complex has been shown to interact in vitro and in cells with a conserved BC-box motif found in an increasing number of proteins including RNA polymerase II elongation factor Elongin A, suppressor of cytokine signaling (SOCS)box proteins, and the von Hippel-Lindau tumor suppressor protein.

The heterodimeric Elongin BC complex has been shown to interact in vitro and in cells with a conserved BC-box motif found in an increasing number of proteins including RNA polymerase II. The heterodimeric Elongin BC complex has been shown to interact tul in vitro and in cells with a conserved BC-box motif found in an bo increasing number of proteins including RNA polymerase II elon- El gation factor Elongin A, suppressor of cytokine signaling (SOCS)- El.

Analysis of the crystal structures of the ternary complexes of BC-box proteins with Elongin BC has revealed that binding of Elongin BC to BC-boxes, which adopt a helical structure, is governed by interaction of an invariant leucine at the N terminus of the BC-box with a hydrophobic pocket created by residues in the C-terminal half of Elongin C.A growing body of evidence has implicated members of the families of Cullin 2 (Cul2)- and Cullin 5 (Cul5)-containing E3 ubiquitin ligases in regulation of diverse cellular processes including cell signaling, growth, and differentiation (reviewed in Ref.

().Cul2 and Cul5 ubiquitin ligases each include the heterodimeric Elongin BC complex, composed of the amino acid Elongin C protein, which. Human Elongin B and C were originally identified as part of the heterotrimeric transcription factor Elongin ABC complex 1 which promotes elongation during transcription by suppressing pausing of RNA polymerase II.

2 Elongin B and C also have the ability to form the heterodimeric Elongin BC complex which associates with cellular proteins that contain a Suppressor Of Cytokine Signaling (SOCS) box .