Interaction of casein kinase II with ribosomal protein L22 of Drosophila melanogaster.

Abstract:

:The ubiquitous eukaryotic protein kinase CKII (casein kinase II) has been found to interact with a number of cellular proteins, either through the catalytic subunit or the regulatory subunit. Using the yeast two-hybrid screening method, we found that the catalytic subunit of Drosophila melanogaster CKII (DmCKII) interacts with Drosophila ribosomal protein L22 (rpL22). This interaction was also observed in vitro with a glutathione-S-transferase (GST)-rpL22 fusion protein. The predicted full-length Drosophila rpL22 protein has an N-terminal extension rich in alanine, lysine, and proline that appears to be unique to Drosophila. Deletion mapping revealed that the conserved core of rpL22 is responsible for the interaction with CKII. Moreover, purified DmCKII can phosphorylate a GST-L22 fusion protein at the C-terminal end, suggesting that this protein may be a substrate of CKII in Drosophila.

authors

Zhao W,Bidwai AP,Glover CV

doi

10.1016/s0006-291x(02)02396-3

subject

Has Abstract

pub_date

2002-10-18 00:00:00

pages

60-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X02023963

journal_volume

298

pub_type

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