Saveanu C, et al. (2007) The p21-activated protein kinase inhibitor Skb15 and its budding yeast homologue are 60S ribosome assembly factors. Mol Cell Biol 27(8):2897-909
Abstract: Ribosome biogenesis is driven by a large number of pre-ribosomal factors that associate to and dissociate from the pre-ribosomal particles along the maturation pathway. We have previously shown that budding yeast Mak11, whose homologues in other eukaryotes were described as modulating a p21-activated protein kinase function, accumulates in Rlp24 associated pre-60S complexes when their maturation is impeded in S. cerevisiae. The functional inactivation of Mak11 interfered with the 60S ribosomal RNA maturation, led to a cell cycle delay in G1 and blocked Rpl25-GFP in the nucleoli of yeast cells, indicating an early role of Mak11 in ribosome assembly. Surprisingly, Mak11 inactivation also led to a dramatic destabilization of Rlp24. The suppression of the thermosensitive phenotype of a mak11 mutant by RLP24 overexpression and a direct in vitro interaction between Rlp24 and Mak11 suggest that Mak11 acts as an Rlp24 co-factor during early steps of 60S ribosomal subunit assembly. Moreover, we found that Skb15, the Mak11 homologue in S. pombe, also associated with pre-ribosomes and affected 60S biogenesis in fission yeast. It is thus likely that the previously observed phenotypes for MAK11 homologues in other eukaryotes are secondary to the main function of these proteins in ribosome formation.
|Status: Published||Type: Journal Article||PubMed ID: 17308036|
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