Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaebacteria, eubacteria, and eucaryotes

Abstract

The genes corresponding to the L10 and L12 equivalent ribosomal proteins (L10e and L12e) of Escherichia coli have been cloned and sequenced from two widely divergent species of archaebacteria, Halobacterium cutirubrum and Sulfolobus solfataricus. The deduced amino acid sequences of the L10e and L12e proteins have been compared to each other and to available eubacterial and eucaryotic sequences. We have identified the human P0 protein as the eucaryotic L10e. The L10e proteins from the three kingdoms were found to be colinear. The eubacterial L10e protein is much shorter than the archaebacterial-eucaryotic proteins because of two large deletions, one internal and one at the carboxy terminus. The archaebacterial and eucaryotic L12e proteins were also colinear; the eubacterial protein is homologous to the archaebacterial and eucaryotic L12e proteins, but has suffered rearrangement through what appear to be gene fusion events. Intraspecies comparisons between L10e and L12e sequences indicate the archaebacterial and eucaryotic L10e proteins contain a partial copy of the L12e protein fused to their carboxy terminus. In the eubacteria most of this fusion has been removed by the carboxy terminal deletion. Within the L12e-derived region, a 26-amino acid-long internal modular sequence reiterated thrice in the archaebacterial L10e, twice in the eucaryotic L10e, and once in the eubacterial L10e was discovered. This modular sequence also appears to be present as a single copy in all L12e proteins and may play a role in L12e dimerization, L10e-L12e complex formation, and the function of L10e-L12e complex in translation.(ABSTRACT TRUNCATED AT 250 WORDS)

Mass Spectrometry Defines the Stoichiometry of Ribosomal Stalk Complexes across the Phylogenetic Tree

“…In yeast, but not in higher eukaryotes, P1 and P2 have both evolved into two ␣ and ␤ proteins (6). In archaea the stalk complex constituents, although named L10 and L12, share sequence homology with the P-proteins (7). L12 and its P1/P2 counterparts are the only ribosomal proteins that have acidic pI values, do not interact directly with rRNA, and are present in multiple copies on the ribosome.…”

Asymmetric Interactions between the Acidic P1 and P2 Proteins in the Saccharomyces cerevisiae Ribosomal Stalk

“…However, the eukaryotic pentamer is less stable and, in contrast to the bacterial pentamer, is readily disassembled by treating the ribosome with ammonium/ethanol buffers (8). The amino acid sequence similarity of the prokaryotic and eukaryotic stalk components is rather low (24). Their structural differences are especially remarkable in the case of P0, which is larger than L10 and contains a carboxyl-end extension of around 100 amino acids not present in the bacterial polypeptide (24).…”

Acidic ribosomal proteins and histone H3 from Leishmania present a high rate of divergence

“…These conserved proteins are placed in the large ribosomal sub-unit forming a highly flexible lateral projection referred as the ribosomal stalk (Wittman 1983, Lake 1985. The stalk is involved in the interaction between the translation factors and the ribosome during protein synthesis (Shimmin et al 1989).Acidic ribosomal P1 protein in trypanosomatids had not been reported in the Leishmania genus previous to this work. However, the P0 and P2 ribosomal proteins had been characterised in L. infantum (Soto et al 1995a, b), L. chagasi (Skeiky et al 1994) and L. donovani (Kunz et al 1993).…”

“…These conserved proteins are placed in the large ribosomal sub-unit forming a highly flexible lateral projection referred as the ribosomal stalk (Wittman 1983, Lake 1985. The stalk is involved in the interaction between the translation factors and the ribosome during protein synthesis (Shimmin et al 1989).…”