Evolutionary relationship and secondary structure predictions in four transport proteins ofSaccharomyces cerevisiae (original) (raw)

Summary

The comparison of the amino acid sequences of four yeast transport proteins indicates that there is a questionable relatedness between the uracil permease (FUR4) and the purine-cytosine permease (FCY2), whereas the arginine permease (CAN1) and the histidine permease (HIP1) clearly originated from a common molecular ancestor. The analysis of the primary structure of these transport proteins by two methods of secondary structure predictions suggests the presence of 9–12 membrane-spanning α-helices in each polypeptide chain. These results are concordant in that 90% of the α-helices were determined by both methods to be at the same positions. In the aligned sequences_HIP1_ and_CAN1_, the postulated membrane-spanning α-helices often start at corresponding sites, even though the overall sequence similarity of the two proteins is only 30%. In the aligned DNA coding sequences of_CAN1_ and_HIP1_, synonymous nucleotide substitutions occur with very similar frequencies in regions where the replacement substitution (changing the amino acids) frequencies are widely different. Moreover, our data suggest that the replacement substitutions can be considered as neutral in the N-terminal segment, whereas the other regions are subject to a conservative selective pressure because, if compared to a random drift, the replacement substitutions are underrepresented.

Access this article

Log in via an institution

Subscribe and save

• Get 10 units per month
• Download Article/Chapter or eBook
• 1 Unit = 1 Article or 1 Chapter
• Cancel anytime Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

• Ahmad M, Bussey H (1986) Yeast arginine permease: nucleotide sequence of the_CAN1_ gene. Curr Genet 10:587–592
  PubMed Google Scholar
• Barker WC, Dayhoff MO (1972) Detecting distant relationships: computer methods and results. In: Dayhoff MO (ed) Atlas of protein sequence and structure, vol 5. National Biomedical Research Foundation, Washington DC, pp 101–110
  Google Scholar
• Cooper TG (1982) Transport in_Saccharomyces cerevisiae_. In: Strathern JN, Jones EW, Broach JR (eds) Molecular biology of the yeast_Saccharomyces cerevisiae_. Metabolism and gene expression. Cold Spring Harbor Laboratory, Cold Spring Harbor NY, pp 399–461
  Google Scholar
• Dayhoff MO, Eck RV, Park CM (1972) A model of evolutionary change in proteins. In: Dayhoff MO (ed) Atlas of protein sequence and structure, vol 5. National Biomedical Research Foundation, Washington DC, pp 89–99
  Google Scholar
• Dayhoff MO, Schwartz RM, Orcutt BC (1978) A model of evolutionary change in proteins. In: Dayhoff MO (ed) Atlas of protein sequence and structure, vol 5, suppl 3. National Biomedical Research Foundation, Washington DC, pp 345–352
  Google Scholar
• Doolittle RF (1981) Similar amino acid sequences: chance or common ancestry? Science 214:149–159
  PubMed Google Scholar
• Eisenberg D, Schwarz E, Komaromy M, Wall R (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179:125–142
  PubMed Google Scholar
• Engelman DM, Steitz TA, Goldman A (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu Rev Biophys Biophys Chem 15:321–353
  PubMed Google Scholar
• Gustafsson K, Wiman K, Emmoth E, Larhammar D, Bohme J, Hyldig-Nielsen JJ, Ronne H, Peterson PA, Rask L (1984) Mutations and selection in the generation of class II histocompatibility antigen polymorphism. EMBO J 3:1655–1661
  PubMed Google Scholar
• Higgins CF, Hiles ID, Salmond GPC, Gill DR, Downie JA, Evans IJ, Holland IB, Gray L, Buckel SD, Bell AW, Hermodson MA (1986) A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature 323:448–450
  PubMed Google Scholar
• Hoffmann W (1985) Molecular characterization of the_CAN1_ locus in_Saccharomyces cerevisiae_. J Biol Chem 260:11831–11837
  PubMed Google Scholar
• Jund R, Weber E, Chevallier MR (1988) Primary structure of the uracil transport protein of_Saccharomyces cerevisiae_. Eur J Biochem 171:417–424
  PubMed Google Scholar
• Kaback HR (1986) Active transport in_Escherichia coli_: passage to permease. Annu Rev Biophys Biophys Chem 15:279–319
  PubMed Google Scholar
• Kimura M (1983) The neutral theory of molecular evolution. Cambridge University Press, Cambridge, England
  Google Scholar
• Kopito RR, Lodish HF (1985) Primary structure and transmembrane orientation of the murine anion exchange protein. Nature 316:234–238
  PubMed Google Scholar
• Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105–132
  PubMed Google Scholar
• Maizel JV Jr, Lenk RP (1981) Enhanced graphic matrix analysis of nucleic acid and protein sequences. Proc Natl Acad Sci USA 78:7665–7669
  PubMed Google Scholar
• Mueckler M, Caruso C, Baldwin SA, Panico M, Blench I, Morris HR, Allard WJ, Lienhard GE, Lodish HF (1985) Sequence and structure of a human glucose transporter. Science 229: 941–945
  PubMed Google Scholar
• Needleman SB, Wunsch CD (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 48:443–453
  PubMed Google Scholar
• Paul C, Rosenbusch JP (1985) Folding patterns of porin and bacteriorhodopsin. EMBO J 4:1593–1597
  PubMed Google Scholar
• Perler F, Efstratiadis A, Lomedico P, Gilbert W, Kolodner R, Dodgson J (1980) The evolution of genes: the chicken preproinsulin gene. Cell 20:555–566
  PubMed Google Scholar
• Schmidt R, Manolson MF, Chevallier MR (1984) Photoaffinity labeling and characterization of the cloned purine-cytosine transport system in_Saccharomyces cerevisiae_. Proc Natl Acad Sci USA 81:6276–6280
  PubMed Google Scholar
• Serrano R, Kielland-Brandt MC, Fink GR (1986) Yeast plasma membrane ATPase is essential for growth and has homology with (Na++K+), K+- and Ca2+-ATPases. Nature 319:689–693
  PubMed Google Scholar
• Smith TF, Waterman MS (1981) Identification of common molecular subsequences. J Mol Biol 147:195–197
  PubMed Google Scholar
• Stroud RM, Finer-Moore J (1985) Acetylcholine receptor structure, function, and evolution. Annu Rev Cell Biol 1:317–351
  PubMed Google Scholar
• Tanaka J, Fink GR (1985) The histidine permease gene (HPII) of_Saccharomyces cerevisiae_. Gene 38:205–214
  PubMed Google Scholar
• Wilbur WJ, Lipman DJ (1983) Rapid similarity searches of nucleic acid and protein data banks. Proc Natl Acad Sci USA 80:726–730
  PubMed Google Scholar
• Wright JK, Seckler R, Overath P (1986) Molecular aspects of sugar: ion cotransport. Annu Rev Biochem 55:225–248
  PubMed Google Scholar

Download references

Author information

Authors and Affiliations

1. Laboratoire de Génétique Physiologique, I.B.M.C. du C.N.R.S., 15 rue R. Descartes, 67084, Strasbourg Cedex, France
   Elisabeth Weber, Marie-Renée Chevallier & Richard Jund

Authors

1. Elisabeth Weber
   You can also search for this author inPubMed Google Scholar
2. Marie-Renée Chevallier
   You can also search for this author inPubMed Google Scholar
3. Richard Jund
   You can also search for this author inPubMed Google Scholar

Rights and permissions

About this article

Cite this article

Weber, E., Chevallier, MR. & Jund, R. Evolutionary relationship and secondary structure predictions in four transport proteins of_Saccharomyces cerevisiae_.J Mol Evol 27, 341–350 (1988). https://doi.org/10.1007/BF02101197

Download citation

• Received: 15 June 1987
• Revised: 05 December 1987
• Accepted: 05 December 1987
• Issue Date: August 1988
• DOI: https://doi.org/10.1007/BF02101197

Key words