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Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds.

Publication ,  Journal Article
Kaufman, JF; Krangel, MS; Strominger, JL
Published in: J Biol Chem
June 10, 1984

Exogenous radioactive palmitic acid is incorporated post-translationally into the HLA-B and -DR heavy chains, but not HLA-A heavy chains or -DR light chains of the human B lymphoblastoid cells JY and T51 . Protease digestions localize the label to the transmembrane region of the B7 heavy chain. Both B7 and DR heavy chains have a cysteine in the transmembrane hydrophobic region, while the A2 heavy chain and DR light chains have none. Palmitic acid is covalently linked to these transmembrane cysteines via a thioester bond since: 1) the label is not removed by organic extraction or boiling in sodium dodecyl sulfate and dithiothreitol, but is released at room temperature by methanolic KOH as methyl palmitate, and by hydroxylamine as palmitohydroxamate . 2) The pH sensitivity and kinetics of release by hydroxylamine and Tris are similar to those of palmitoyl-CoA (thioester linkage) and unlike those of methyl palmitate and palmitoyllysophosphatidylcholine ( hydroxyester linkages). 3) Neutral hydroxylamine treatment (but not neutral Tris treatment) generates sites that can be reduced and alkylated in the transmembrane region of B7 heavy chain and to a lesser extent in DR heavy chain. 4) Organic extraction of pronase digests of labeled B7 yields peptides containing palmitate and cysteine (but not serine or threonine) which co-migrate by thin layer chromatography. A population of beta 2-microglobulin molecules not associated with heavy chains is palmitylated , but not via a thioester linkage.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

June 10, 1984

Volume

259

Issue

11

Start / End Page

7230 / 7238

Location

United States

Related Subject Headings

  • Tromethamine
  • Peptide Hydrolases
  • Palmitoyl Coenzyme A
  • Palmitic Acids
  • Palmitic Acid
  • Major Histocompatibility Complex
  • Hydroxylamines
  • Hydroxylamine
  • Hydrogen-Ion Concentration
  • Humans
 

Citation

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Kaufman, J. F., Krangel, M. S., & Strominger, J. L. (1984). Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds. J Biol Chem, 259(11), 7230–7238.
Kaufman, J. F., M. S. Krangel, and J. L. Strominger. “Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds.J Biol Chem 259, no. 11 (June 10, 1984): 7230–38.
Kaufman JF, Krangel MS, Strominger JL. Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds. J Biol Chem. 1984 Jun 10;259(11):7230–8.
Kaufman, J. F., et al. “Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds.J Biol Chem, vol. 259, no. 11, June 1984, pp. 7230–38.
Kaufman JF, Krangel MS, Strominger JL. Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds. J Biol Chem. 1984 Jun 10;259(11):7230–7238.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

June 10, 1984

Volume

259

Issue

11

Start / End Page

7230 / 7238

Location

United States

Related Subject Headings

  • Tromethamine
  • Peptide Hydrolases
  • Palmitoyl Coenzyme A
  • Palmitic Acids
  • Palmitic Acid
  • Major Histocompatibility Complex
  • Hydroxylamines
  • Hydroxylamine
  • Hydrogen-Ion Concentration
  • Humans