Purification and Characterization of Protein Synthesis Initiation Factor eIF-4E from the Yeast Saccharomyces cerevisiae

Michael Altmann; Hans Trachsel; Isaac Edery; Nahum Sonenberg

doi:10.1021/bi00343a009

Purification and Characterization of Protein Synthesis Initiation Factor eIF-4E from the Yeast Saccharomyces cerevisiae

Michael Altmann, Hans Trachsel, Isaac Edery, Nahum Sonenberg

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51 Scopus citations

Abstract

A 24 000-dalton protein [yeast eukaryotic initiation factor 4E (eIF-4E)] was purified from yeast Saccharomyces cerevisiae postribosomal supernatant by m7GDP-agarose affinity chromatography. The protein behaves very similarly to mammalian protein synthesis initiation factor eIF-4E with respect to (i) binding to and elution from m7GDP-agarose columns and (ii) cross-linking to oxidized reovirus mRNA cap structures. Yeast eIF-4E is required for translation as shown by the strong and specific inhibition of cell-free translation in a yeast extract by a monoclonal antibody directed against yeast eIF-4E.

Original language	English (US)
Pages (from-to)	6085-6089
Number of pages	5
Journal	Biochemistry
Volume	24
Issue number	22
DOIs	https://doi.org/10.1021/bi00343a009
State	Published - Oct 1 1985
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi00343a009

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title = "Purification and Characterization of Protein Synthesis Initiation Factor eIF-4E from the Yeast Saccharomyces cerevisiae",

abstract = "A 24 000-dalton protein [yeast eukaryotic initiation factor 4E (eIF-4E)] was purified from yeast Saccharomyces cerevisiae postribosomal supernatant by m7GDP-agarose affinity chromatography. The protein behaves very similarly to mammalian protein synthesis initiation factor eIF-4E with respect to (i) binding to and elution from m7GDP-agarose columns and (ii) cross-linking to oxidized reovirus mRNA cap structures. Yeast eIF-4E is required for translation as shown by the strong and specific inhibition of cell-free translation in a yeast extract by a monoclonal antibody directed against yeast eIF-4E.",

author = "Michael Altmann and Hans Trachsel and Isaac Edery and Nahum Sonenberg",

year = "1985",

month = oct,

day = "1",

doi = "10.1021/bi00343a009",

language = "English (US)",

volume = "24",

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journal = "Biochemistry",

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T1 - Purification and Characterization of Protein Synthesis Initiation Factor eIF-4E from the Yeast Saccharomyces cerevisiae

AU - Altmann, Michael

AU - Trachsel, Hans

AU - Edery, Isaac

AU - Sonenberg, Nahum

PY - 1985/10/1

Y1 - 1985/10/1

N2 - A 24 000-dalton protein [yeast eukaryotic initiation factor 4E (eIF-4E)] was purified from yeast Saccharomyces cerevisiae postribosomal supernatant by m7GDP-agarose affinity chromatography. The protein behaves very similarly to mammalian protein synthesis initiation factor eIF-4E with respect to (i) binding to and elution from m7GDP-agarose columns and (ii) cross-linking to oxidized reovirus mRNA cap structures. Yeast eIF-4E is required for translation as shown by the strong and specific inhibition of cell-free translation in a yeast extract by a monoclonal antibody directed against yeast eIF-4E.

AB - A 24 000-dalton protein [yeast eukaryotic initiation factor 4E (eIF-4E)] was purified from yeast Saccharomyces cerevisiae postribosomal supernatant by m7GDP-agarose affinity chromatography. The protein behaves very similarly to mammalian protein synthesis initiation factor eIF-4E with respect to (i) binding to and elution from m7GDP-agarose columns and (ii) cross-linking to oxidized reovirus mRNA cap structures. Yeast eIF-4E is required for translation as shown by the strong and specific inhibition of cell-free translation in a yeast extract by a monoclonal antibody directed against yeast eIF-4E.

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DO - 10.1021/bi00343a009

M3 - Article

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JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

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ER -

Purification and Characterization of Protein Synthesis Initiation Factor eIF-4E from the Yeast Saccharomyces cerevisiae

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