Phosphorylation of wheat germ initiation factors and ribosomal proteins.

Abstract:

:The ability of the wheat germ initiation factors and ribosomes to serve as substrates for a wheat germ protein kinase (Yan and Tao 1982 J Biol Chem 257: 7037-7043) has been investigated. The wheat germ kinase catalyzes the phosphorylation of the 42,000 dalton subunit of eukaryotic initiation factor (eIF)-2 and the 107,000 dalton subunit of eIF-3. Other initiation factors, eIF-4B and eIF-4A, and elongation factors, EF-1 and EF-2, are not phosphorylated by the kinase. Quantitative analysis indicates that the kinase catalyzes the incorporation of about 0.5 to 0.6 mole of phosphate per mole of the 42,000 dalton subunit of eIF-2 and about 6 moles of phosphate per mole of the 107,000 dalton subunit of eIF-3. Three proteins (M(r) = 38,000, 14,800, and 12,600) of the 60S ribosomal subunit are phosphorylated by the kinase, but none of the 40S ribosomal proteins are substrates of the kinase. No effects of phosphorylation on the activities of eIF-2, eIF-3, or 60S ribosomal subunits could be demonstrated in vitro.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Browning KS,Yan TF,Lauer SJ,Aquino LA,Tao M,Ravel JM

doi

10.1104/pp.77.2.370

subject

Has Abstract

pub_date

1985-02-01 00:00:00

pages

370-3

issue

2

eissn

0032-0889

issn

1532-2548

journal_volume

77

pub_type

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