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Synthesis and Phosphorylation of Maize Acidic Ribosomal Proteins1
Implications in Translational Regulation

Raúl Aguilar, Leonel Montoya, and Estela Sánchez de Jiménez*

Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, D.F. 04510, México

The objective of this research was to determine the role of acidic ribosomal protein (ARP) phosphorylation in translation. Ribosomes (Rbs) from germinated maize (Zea mays L.) axes had four ARP bands within 4.2 to 4.5 isoelectric points when analyzed by isoelectric focusing. Two of these bands disappeared after alkaline phosphatase hydrolysis. During germination a progressive change from nonphosphorylated (0 h) to phosphorylated ARP (24 h) forms was observed in the Rbs; a free cytoplasmic pool of nonphosphorylated ARPs was also identified by immunoblot and isoelectric focusing experiments. De novo ARP synthesis initiated very slowly early in germination, whereas ARP phosphorylation occurred rapidly within this period. ARP-phosphorylated versus ARP-nonphosphorylated Rbs were tested in an in vitro reticulocyte lysate translation system. Greater in vitro mRNA translation rates were demonstrated for the ARP-phosphorylated Rbs than for the non-ARP-phosphorylated ones. Rapamycin application to maize axes strongly inhibited S6 ribosomal protein phosphorylation, but did not interfere with the ARP phosphorylation reaction. We conclude that ARP phosphorylation does not depend on ARP synthesis or on ARP assembly into Rbs. Rather, this process seems to be part of a translational regulation mechanism.

1   This work was supported by the Dirección General de Asuntos del Personal Académico, Universidad Nacional Autonoma de Mexico (grant nos. IN200793 and IN217496).
*   Corresponding author; e-mail estelas{at}servidor.unam.mx; fax 52-5-6-22-53-29.

Plant Physiol. (1998) 116: 379-385
Copyright Clearance Center:   0032-0889/98/116/0379/07
© 1998 American Society of Plant Physiologists




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