The assembly factor Erb1 functions in multiple remodeling events during 60S ribosomal subunit assembly in S. cerevisiae.

A major gap in our understanding of ribosome assembly is knowing the precise function of each of the ∼200 assembly factors. The steps in subunit assembly in which these factors participate have been examined for the most part by depleting each protein from cells. Depletion of the assembly factor Erb1 prevents stable assembly of seven other interdependent assembly factors with pre-60S subunits, resulting in turnover of early preribosomes, before the ITS1 spacer can be removed from 27SA3 pre-rRNA.

Principles of 60S ribosomal subunit assembly emerging from recent studies in yeast.

Ribosome biogenesis requires the intertwined processes of folding, modification, and processing of ribosomal RNA, together with binding of ribosomal proteins. In eukaryotic cells, ribosome assembly begins in the nucleolus, continues in the nucleoplasm, and is not completed until after nascent particles are exported to the cytoplasm. The efficiency and fidelity of ribosome biogenesis are facilitated by >200 assembly factors and ∼76 different small nucleolar RNAs.

Ytm1, Nop7, and Erb1 form a complex necessary for maturation of yeast 66S preribosomes.

The essential, conserved yeast nucleolar protein Ytm1 is one of 17 proteins in ribosome assembly intermediates that contain WD40 protein-protein interaction motifs. Such proteins may play key roles in organizing other molecules necessary for ribosome biogenesis. Ytm1 is present in four consecutive 66S preribosomes containing 27SA2, 27SA3, 27SB, and 25.

Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation.

The Saccharomyces cerevisiae gene RRP1 encodes an essential, evolutionarily conserved protein necessary for biogenesis of 60S ribosomal subunits. Processing of 27S pre-ribosomal RNA to mature 25S rRNA is blocked and 60S subunits are deficient in the temperature-sensitive rrp1-1 mutant. We have used recent advances in proteomic analysis to examine in more detail the function of Rrp1p in ribosome biogenesis.

Interactions of yeast ribosomal protein rpS14 with RNA.

Yeast ribosomal protein S14 (rpS14) binds to two different RNA molecules: (1). helix 23 of 18S rRNA during its assembly into 40S ribosomal subunits and (2). a stem-loop structure in RPS14B pre-mRNA to repress expression of the RPS14B gene.

Chaperoning ribosome assembly.

Reconstitution of bacterial ribosomes in vitro from RNA and protein constituents requires a heating step to rearrange conformation of an intermediate. In this issue of Molecular Cell, Maki et al. demonstrate that the DnaK chaperone system circumvents the requirement for heating.