Literature DB >> 8051015

Phylogenetic analysis of sequences from diverse bacteria with homology to the Escherichia coli rho gene.

T Opperman1, J P Richardson.   

Abstract

Genes from Pseudomonas fluorescens, Chromatium vinosum, Micrococcus luteus, Deinococcus radiodurans, and Thermotoga maritima with homology to the Escherichia coli rho gene were cloned and sequenced, and their sequences were compared with other available sequences. The species for all of the compared sequences are members of five bacterial phyla, including Thermotogales, the most deeply diverged phylum. This suggests that a rho-like gene is ubiquitous in the Bacteria and was present in their common ancestor. The comparative analysis revealed that the Rho homologs are highly conserved, exhibiting a minimum identity of 50% of their amino acid residues in pairwise comparisons. The ATP-binding domain had a particularly high degree of conservation, consisting of some blocks with sequences of residues that are very similar to segments of the alpha and beta subunits of F1-ATPase and of other blocks with sequences that are unique to Rho. The RNA-binding domain is more diverged than the ATP-binding domain. However, one of its most highly conserved segments includes a RNP1-like sequence, which is known to be involved in RNA binding. Overall, the degree of similarity is lowest in the first 50 residues (the first half of the RNA-binding domain), in the putative connector region between the RNA-binding and the ATP-binding domains, and in the last 50 residues of the polypeptide. Since functionally defective mutants for E. coli Rho exist in all three of these segments, they represent important parts of Rho that have undergone adaptive evolution.

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Year:  1994        PMID: 8051015      PMCID: PMC196342          DOI: 10.1128/jb.176.16.5033-5043.1994

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  40 in total

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4.  Site-directed alterations in the ATP-binding domain of rho protein affect its activities as a termination factor.

Authors:  A J Dombroski; C A Brennan; P Spear; T Platt
Journal:  J Biol Chem       Date:  1988-12-15       Impact factor: 5.157

5.  A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein.

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6.  Progressive sequence alignment as a prerequisite to correct phylogenetic trees.

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8.  The ATP binding site on rho protein. Affinity labeling of Lys181 by pyridoxal 5'-diphospho-5'-adenosine.

Authors:  A J Dombroski; J R LaDine; R L Cross; T Platt
Journal:  J Biol Chem       Date:  1988-12-15       Impact factor: 5.157

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Authors:  A J Dombroski; T Platt
Journal:  Proc Natl Acad Sci U S A       Date:  1988-04       Impact factor: 11.205

10.  Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes.

Authors:  J P Gogarten; H Kibak; P Dittrich; L Taiz; E J Bowman; B J Bowman; M F Manolson; R J Poole; T Date; T Oshima; J Konishi; K Denda; M Yoshida
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  19 in total

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2.  Substrate specificities and expression patterns reflect the evolutionary divergence of maltose ABC transporters in Thermotoga maritima.

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Review 4.  Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes.

Authors:  R S Gupta
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Authors:  N Promadej; F Fiedler; P Cossart; S Dramsi; S Kathariou
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6.  SraL sRNA interaction regulates the terminator by preventing premature transcription termination of rho mRNA.

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7.  Mutations in the primary sigma factor σA and termination factor rho that reduce susceptibility to cell wall antibiotics.

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8.  rho is not essential for viability or virulence in Staphylococcus aureus.

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10.  Binding and translocation of termination factor rho studied at the single-molecule level.

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