Literature DB >> 3541205

Many random sequences functionally replace the secretion signal sequence of yeast invertase.

C A Kaiser, D Preuss, P Grisafi, D Botstein.   

Abstract

In the process of protein secretion, amino-terminal signal sequences are key recognition elements; however, the relation between the primary sequence of an amino-terminal peptide and its ability to function as an export signal remains obscure. The limits of variation permitted for functional signal sequences were determined by replacement of the normal signal sequence of Saccharomyces cerevisiae invertase with essentially random peptide sequences. Since about one-fifth of these sequences can function as an export signal the specificity with which signal sequences are recognized must be very low.

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Year:  1987        PMID: 3541205     DOI: 10.1126/science.3541205

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  124 in total

1.  Signal-exon trap: a novel method for the identification of signal sequences from genomic DNA.

Authors:  M Péterfy; T Gyuris; L Takács
Journal:  Nucleic Acids Res       Date:  2000-04-01       Impact factor: 16.971

2.  Engineered viruses to select genes encoding secreted and membrane-bound proteins in mammalian cells.

Authors:  Pierre Moffatt; Patrick Salois; Marie-Hélène Gaumond; Natalie St-Amant; Eric Godin; Christian Lanctôt
Journal:  Nucleic Acids Res       Date:  2002-10-01       Impact factor: 16.971

Review 3.  The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology.

Authors:  Christopher J Guerriero; Jeffrey L Brodsky
Journal:  Physiol Rev       Date:  2012-04       Impact factor: 37.312

Review 4.  Current views on chloroplast protein import and hypotheses on the origin of the transport mechanism.

Authors:  E K Archer; K Keegstra
Journal:  J Bioenerg Biomembr       Date:  1990-12       Impact factor: 2.945

Review 5.  Intracellular traffic of newly synthesized proteins. Current understanding and future prospects.

Authors:  V R Lingappa
Journal:  J Clin Invest       Date:  1989-03       Impact factor: 14.808

6.  Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide.

Authors:  J W Puziss; J D Fikes; P J Bassford
Journal:  J Bacteriol       Date:  1989-05       Impact factor: 3.490

7.  Mouse brain CD4 transcripts encode only the COOH-terminal half of the protein.

Authors:  N Lonberg; S N Gettner; E Lacy; D R Littman
Journal:  Mol Cell Biol       Date:  1988-05       Impact factor: 4.272

8.  A signal peptide secretion screen in Fucus distichus embryos reveals expression of glucanase, EGF domain-containing, and LRR receptor kinase-like polypeptides during asymmetric cell growth.

Authors:  Kenneth D Belanger; Aaron J Wyman; Michelle N Sudol; Sneh L Singla-Pareek; Ralph S Quatrano
Journal:  Planta       Date:  2003-06-27       Impact factor: 4.116

9.  Influence of N-terminal truncations on the functional expression of Bacillus licheniformis gamma-glutamyltranspeptidase in recombinant Escherichia coli.

Authors:  Long-Liu Lin; Li-Yu Yang; Hui-Yu Hu; Huei-Fen Lo
Journal:  Curr Microbiol       Date:  2008-09-23       Impact factor: 2.188

10.  The effect of α-mating factor secretion signal mutations on recombinant protein expression in Pichia pastoris.

Authors:  Geoff P Lin-Cereghino; Carolyn M Stark; Daniel Kim; Jennifer Chang; Nadia Shaheen; Hansel Poerwanto; Kimiko Agari; Pachai Moua; Lauren K Low; Namphuong Tran; Amy D Huang; Maria Nattestad; Kristin T Oshiro; John William Chang; Archana Chavan; Jerry W Tsai; Joan Lin-Cereghino
Journal:  Gene       Date:  2013-02-21       Impact factor: 3.688

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