Abstract

The genomic associations of the archaeal ribosomal proteins, (r-proteins), were examined in detail. The archaeal versions of the universal r-protein genes are typically in clusters similar or identical and to those found in bacteria. Of the 35 nonuniversal archaeal r-protein genes examined, the gene encoding L18e was found to be associated with the conserved L13 cluster, whereas the genes for S4e, L32e and L19e were found in the archaeal version of the spc operon. Eleven nonuniversal protein genes were not associated with any common genomic context. Of the remaining 19 protein genes, 17 were convincingly assigned to one of 10 previously unrecognized gene clusters. Examination of the gene content of these clusters revealed multiple associations with genes involved in the initiation of protein synthesis, transcription or other cellular processes. The lack of such associations in the universal clusters suggests that initially the ribosome evolved largely independently of other processes. More recently it likely has evolved in concert with other cellular systems. It was also verified that a second copy of the gene encoding L7ae found in some bacteria is actually a homolog of the gene encoding L30e and should be annotated as such.

Highlights

  • The archaeal translation machinery has a long evolutionary history and it is of interest to know how it have evolved and how its interactions with other cellular processes have changed over time (Fox and Naik 2004)

  • In the work reported here, we identified previously unrecognized genomic associations of ribosomal proteins (r-proteins) in archaea and discuss the implications of these associations for the early history of the translation machinery

  • In the work presented here, we investigated the genomic associations of each of these proteins and identified 10 previously unrecognized, but significantly conserved gene clusters

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Summary

Introduction

The archaeal translation machinery has a long evolutionary history and it is of interest to know how it have evolved and how its interactions with other cellular processes have changed over time (Fox and Naik 2004). 17 large subunit and 19 small subunit r-proteins are universal These 36 r-proteins likely appeared before the last common ancestor, (LUCA), and are considered to be ancient in origin (Kyrpides et al 1999, Lecompte et al 2002). The Archaea and the Eucaryota share 11 large subunit (LSU) r-proteins and 20 small subunit (SSU) r-proteins but share no r-protein with the Bacteria other than the universal proteins (Lecompte et al 2002). The large numbers of r-protein families shared by the Archaea and the Eucaryota suggest that the eukaryotic translation system originated from an archaeal version (Hartman et al 2006)

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