2 edition of Role of the accessory proteins tapasin and Bap29/31 in the biogenesis of MHC class I molecules. found in the catalog.
Role of the accessory proteins tapasin and Bap29/31 in the biogenesis of MHC class I molecules.
Written in English
Class I histocompatibility molecules, consisting of a heavy chain, a light chain (beta2-microglobulin) and peptide, are assembled in the endoplasmic reticulum before being exported to the Golgi apparatus and the cell surface where they are surveyed by cytotoxic T cells. Assembly of the heavy/light chain heterodimer with peptide occurs in the peptide loading complex, which consists of the transporter associated with antigen processing, tapasin, ERp57, calnexin and calreticulin. In the first part of this thesis, I have used a mutational approach to investigate the physical organization of the peptide loading complex with a particular emphasis on tapasin. Several residues were identified to be involved in the interaction between H-2 D d and tapasin and mutations at these positions resulted in phenotypes of low surface expression, altered endoplasmic reticulum to Golgi transport and mildly affected peptide loading. These complex observations, analyzed in the context of similar studies performed with HLA-A2 and H-2 Ld suggest that the organization of the peptide loading complex can vary depending on the specific class I molecule examined. In the second part of this thesis, I investigated later events in the biogenesis of class I molecules, namely their export from the endoplasmic reticulum to the Golgi apparatus. I found that the putative cargo receptor Bap31 binds to two allotypes of mouse class I molecules with the interaction initiated at the time of heavy chain association with beta2-microglobulin and maintained until the class I molecule has left the endoplasmic reticulm. Consistent with an important role in recruiting class I molecules to transport vesicles, I showed that in the absence of Bap31 and its binding partner Bap29, there is a loss of class I colocalization with p137, a component of mammalian COPII coats. This observation is also associated with a delay in class I traffic from the endoplasmic reticulum to the Golgi. These observations are consistent with the view that class I molecules are largely recruited to endoplasmic reticulum exit sites by Bap29/31 and that Bap29/31 is a cargo receptor for major histocompatibility complex class I molecules.
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Introduction. MHC class I molecules present peptides, derived from intracellular proteins, to T cells. The three components of MHC class I molecules, a transmembrane heavy chain, β 2-microglobulin and a peptide, typically 8–10 amino acids, are assembled sequentially in the endoplasmic reticulum (ER) ().When peptide loading is complete, MHC class I molecules are exported from the Cited by: Bap29/31 influences the intracellular traffic of MHC class I molecules.
ImmunolCrossref, Medline, Google Scholar; Puri S., Linstedt A. Capacity of the Golgi apparatus for biogenesis from the endoplasmic reticulum. Mol. Biol. C Link, Google Scholar; Römisch K. Endoplasmic reticulum.
MHC Class I Present in all nucleated cells and platelets (in different density). MHC class II molecule a and b chains Expressed on professional or facultative antigen presenting cells (APCs): •Constitutive •Induced Class I and class II MHC Molecules MHC class I and class II molecules with bound peptides Automated benchmarking of peptide-MHC class I binding predictions.
PubMed. Trolle, Thomas; Metushi, Imir G; Greenbaum, Jason A; Kim, Yohan; Sidney, John; Lund, Ole. Class I MHC Molecules (Chapter 19) Class I MHC molecules are membrane glycoproteins expressed on most cells.
They consist of an α chain of approximat daltons noncovalently associated with β2-microglobulin, a 12,dalton molecule (Figure ). The gene for the α chain is encoded in the MHC, whereas that for β2-microglobulin is not.
Class I and class II major histocompatibility complex (MHC) molecules play significant roles in T cell development and immune function. We show that MHCI- and MHCII-deficient mice have low numbers of macrophage precursors and circulating monocytes, as well as abnormal bone marrow cell colony-stimulating factor type 1 secretion and bone composition.
CA Biological process. // ID Cytochrome c-type biogenesis. AC KW DE Protein involved in the biogenesis of c-type cytochromes. Cytochromes DE c are electron-transfer proteins having one or several heme c groups, DE bound to the protein by one or, more commonly two, thioether bonds DE involving sulphydryl groups of cysteine residues.
Interestingly, the crystallographic structures of class I MHC molecules are similar regardless of the allotype or species of origin [7–16].
Class I MHC molecules are heterotrimeric complexes comprised of a ~kDa heavy chain, a noncovalently bound kDa serum protein, b2-microglobulin (b2m), and a small peptide (Figure a). 1 2 3 4 5 6 7 8 9 10 11 12 13 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 The proteins are secreted in an incompletely folded conformation.
The core β-sheet forms before the rest of the protein folds correctly. The β-sheets from two or more incompletely folded protein molecules associate to begin forming an amyloid fibril.
Additional protein molecules slowly associate with the amyloid and extend it to form a fibril. Journal Article. Wang, Limei; Dorn, Patrick; Zeinali, Soheila; Froment, Laurène; Berezowska, Sabina; Kocher, Gregor J; Alves, Marco P; Brügger, Melanie; Esteves.
Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic." [ISBN] synonym: "enzyme activity" EXACT [GOC:dph, GOC:tb] is_a: GO [Term].
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AUA1 AUA AUA AUA1 AU A1 AU A1 AU A1 AU A AU A AU A AU A AU A AU A AU A1 AU A1 AU A1 Authority AU Australia Prior art keywords protein receptor sequence alpha member.
The invention includes a method of creating an animal or cell with at least one chromosome editing. In particular, the present invention relates to the use of targeted zinc finger nucleases to edit chromosomal sequences.
The invention further includes animals or cells created by the methods of the invention. The present invention encompasses a method for creating an animal or cell with at least one chromosomal edit.
In particular, the invention relates to the use of targeted zinc finger nucleases to edit chromosomal sequences. The invention further encompasses an animal or a.
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BADER Mike BYROM Charles D. JOHNSON David BROWN Agents: Fullbright & Jaworski L.L.P. Assignees: Origin: AUSTIN, TX US IPC8 Class: AA61KFI USPC Class: 44 Abstract: The present invention concerns methods and compositions for identifying genes or .