Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 May;70(5):1526–1530. doi: 10.1073/pnas.70.5.1526

Biosynthesis of Reticulocyte Membrane Proteins by Membrane-Free Polyribosomes

Harvey F Lodish 1
PMCID: PMC433535  PMID: 4514321

Abstract

Intact rabbit reticulocyte cells synthesize two predominant species of membrane polypeptides; at least 10 reticulocyte membrane polypeptide species are not produced by the cells. Cell-free extracts of reticulocytes, free of any membranes or membrane-bound polyribosomes, synthesize large amounts of these two membrane polypeptides; one of these polypeptides appears to be modified, probably by loss of 20-40 amino acids, after it is incorporated into the membrane. Deprivation of hemin results in inhibition of synthesis by lysates of membrane proteins, globin, and all other cytoplasmic proteins.

Keywords: rabbit, hemin, globin, gel electrophoresis

Full text

PDF
1526

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adamson S. D., Herbert E., Godchaux W. Factors affecting the rate of protein synthesis in lysate systems from reticulocytes. Arch Biochem Biophys. 1968 May;125(2):671–683. doi: 10.1016/0003-9861(68)90625-5. [DOI] [PubMed] [Google Scholar]
  2. Adamson S. D., Herbert E., Kemp S. F. Effects of hemin and other porphyrins on protein synthesis in a reticulocyte lysate cell-free system. J Mol Biol. 1969 Jun 14;42(2):247–258. doi: 10.1016/0022-2836(69)90041-2. [DOI] [PubMed] [Google Scholar]
  3. Berg H. C. Sulfanilic acid diazonium salt: a label for the outside of the human erythrocyte membrane. Biochim Biophys Acta. 1969 Jun 3;183(1):65–78. doi: 10.1016/0005-2736(69)90130-8. [DOI] [PubMed] [Google Scholar]
  4. Bretscher M. S. A major protein which spans the human erythrocyte membrane. J Mol Biol. 1971 Jul 28;59(2):351–357. doi: 10.1016/0022-2836(71)90055-6. [DOI] [PubMed] [Google Scholar]
  5. Bretscher M. S. Human erythrocyte membranes: specific labelling of surface proteins. J Mol Biol. 1971 Jun 28;58(3):775–781. doi: 10.1016/0022-2836(71)90039-8. [DOI] [PubMed] [Google Scholar]
  6. Bretscher M. S. Major human erythrocyte glycoprotein spans the cell membrane. Nat New Biol. 1971 Jun 23;231(25):229–232. doi: 10.1038/newbio231229a0. [DOI] [PubMed] [Google Scholar]
  7. Bulova S. I., Burka E. R. Biosynthesis of nonglobin protein by membrane-bound ribosomes in reticulocytes. J Biol Chem. 1970 Oct 10;245(19):4907–4912. [PubMed] [Google Scholar]
  8. Dallner G., Siekevitz P., Palade G. E. Biogenesis of endoplasmic reticulum membranes. I. Structural and chemical differentiation in developing rat hepatocyte. J Cell Biol. 1966 Jul;30(1):73–96. doi: 10.1083/jcb.30.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  10. Ganoza M. C., Williams C. A. In vitro synthesis of different categories of specific protein by membrane-bound and free ribosomes. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1370–1376. doi: 10.1073/pnas.63.4.1370. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gross M., Rabinovitz M. Control of globin synthesis in cell-free preparations of reticulocytes by formation of a translational repressor that is inactivated by hemin. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1565–1568. doi: 10.1073/pnas.69.6.1565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Guidotti G. Membrane proteins. Annu Rev Biochem. 1972;41:731–752. doi: 10.1146/annurev.bi.41.070172.003503. [DOI] [PubMed] [Google Scholar]
  13. Housman D., Jacobs-Lorena M., Rajbhandary U. L., Lodish H. F. Initiation of haemoglobin synthesis by methionyl-tRNA. Nature. 1970 Aug 29;227(5261):913–918. doi: 10.1038/227913a0. [DOI] [PubMed] [Google Scholar]
  14. Howard G. A., Adamson S. D., Herbert E. Studies on cessation of protein synthesis in a reticulocyte lysate cell-free system. Biochim Biophys Acta. 1970 Jul 16;213(1):237–240. doi: 10.1016/0005-2787(70)90028-6. [DOI] [PubMed] [Google Scholar]
  15. Hubbard A. L., Cohn Z. A. The enzymatic iodination of the red cell membrane. J Cell Biol. 1972 Nov;55(2):390–405. doi: 10.1083/jcb.55.2.390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lenard J. Protein components of erythrocyte membranes from different animal species. Biochemistry. 1970 Dec 8;9(25):5037–5040. doi: 10.1021/bi00827a032. [DOI] [PubMed] [Google Scholar]
  17. Lodish H. F. Alpha and beta globin messenger ribonucleic acid. Different amounts and rates of initiation of translation. J Biol Chem. 1971 Dec 10;246(23):7131–7138. [PubMed] [Google Scholar]
  18. Lodish H. F. Bacteriophage f2 RNA: control of translation and gene order. Nature. 1968 Oct 26;220(5165):345–350. doi: 10.1038/220345a0. [DOI] [PubMed] [Google Scholar]
  19. Lodish H. F., Jacobsen M. Regulation of hemoglobin synthesis. Equal rates of translation and termination of - and -globin chains. J Biol Chem. 1972 Jun 10;247(11):3622–3629. [PubMed] [Google Scholar]
  20. Lodish H. F. Secondary structure of bacteriophage f2 ribonucleic acid and the initiation of in vitro protein biosynthesis. J Mol Biol. 1970 Jun 28;50(3):689–702. doi: 10.1016/0022-2836(70)90093-8. [DOI] [PubMed] [Google Scholar]
  21. Lodish H. G., Housman D., Jacobsen M. Initiation of hemoglobin synthesis. Specific inhibition by antibiotics and bacteriophage ribonucleic acid. Biochemistry. 1971 Jun 8;10(12):2348–2356. doi: 10.1021/bi00788a027. [DOI] [PubMed] [Google Scholar]
  22. Maxwell C. R., Rabinovitz M. Evidence for an inhibitor in the control of globin synthesis by hemin in a reticulocyte lysate. Biochem Biophys Res Commun. 1969 Apr 10;35(1):79–85. doi: 10.1016/0006-291x(69)90485-9. [DOI] [PubMed] [Google Scholar]
  23. McDowell M. J., Joklik W. K. An in vitro protein synthesizing system from mouse L fibroblasts infected with reovirus. Virology. 1971 Sep;45(3):724–733. doi: 10.1016/0042-6822(71)90186-3. [DOI] [PubMed] [Google Scholar]
  24. Moss B., Rosenblum E. N. Hydroxylapatite chromatography of protein-sodium dodecyl sulfate complexes. A new method for the separation of polypeptide subunits. J Biol Chem. 1972 Aug 25;247(16):5194–5198. [PubMed] [Google Scholar]
  25. Phillips D. R., Morrison M. Exposed protein on the intact human erythrocyte. Biochemistry. 1971 May 11;10(10):1766–1771. doi: 10.1021/bi00786a006. [DOI] [PubMed] [Google Scholar]
  26. Phillips D. R., Morrison M. Position of glycoprotein polypeptide chain in the human erythrocyte membrane. FEBS Lett. 1971 Oct 15;18(1):95–97. doi: 10.1016/0014-5793(71)80416-7. [DOI] [PubMed] [Google Scholar]
  27. Redman C. M. Biosynthesis of serum proteins and ferritin by free and attached ribosomes of rat liver. J Biol Chem. 1969 Aug 25;244(16):4308–4315. [PubMed] [Google Scholar]
  28. Rosenberg S. A., Guidotti G. Fractionation of the protein components of human erythrocyte membranes. J Biol Chem. 1969 Oct 10;244(19):5118–5124. [PubMed] [Google Scholar]
  29. SIEKEVITZ P., PALADE G. E. A cytochemical study on the pancreas of the guinea pig. 5. In vivo incorporation of leucine-1-C14 into the chymotrypsinogen of various cell fractions. J Biophys Biochem Cytol. 1960 Jul;7:619–630. doi: 10.1083/jcb.7.4.619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Sabatini D. D., Blobel G. Controlled proteolysis of nascent polypeptides in rat liver cell fractions. II. Location of the polypeptides in rough microsomes. J Cell Biol. 1970 Apr;45(1):146–157. doi: 10.1083/jcb.45.1.146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Sabatini D. D., Tashiro Y., Palade G. E. On the attachment of ribosomes to microsomal membranes. J Mol Biol. 1966 Aug;19(2):503–524. doi: 10.1016/s0022-2836(66)80019-0. [DOI] [PubMed] [Google Scholar]
  32. Steck T. L., Fairbanks G., Wallach D. F. Disposition of the major proteins in the isolated erythrocyte membrane. Proteolytic dissection. Biochemistry. 1971 Jun 22;10(13):2617–2624. doi: 10.1021/bi00789a031. [DOI] [PubMed] [Google Scholar]
  33. Trayer H. R., Nozaki Y., Reynolds J. A., Tanford C. Polypeptide chains from human red blood cell membranes. J Biol Chem. 1971 Jul 25;246(14):4485–4488. [PubMed] [Google Scholar]
  34. Warren L., Glick M. C. Membranes of animal cells. II. The metabolism and turnover of the surface membrane. J Cell Biol. 1968 Jun;37(3):729–746. doi: 10.1083/jcb.37.3.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Winzler R. J., Harris E. D., Pekas D. J., Johnson C. A., Weber P. Studies on glycopeptides released by trypsin from intact human erythrocytes. Biochemistry. 1967 Jul;6(7):2195–2202. doi: 10.1021/bi00859a042. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES