Analysis of ancient sequence motifs in the H+‐PPase family

  title={Analysis of ancient sequence motifs in the H+‐PPase family},
  author={Joel Hedlund and Roberto Cantoni and Margareta Baltscheffsky and Herrick Baltscheffsky and Bengt Persson},
  journal={The FEBS Journal},
The unique family of membrane‐bound proton‐pumping inorganic pyrophosphatases, involving pyrophosphate as the alternative to ATP, was investigated by characterizing 166 members of the UniProtKB/Swiss‐Prot + UniProtKB/TrEMBL databases and available completed genomes, using sequence comparisons and a hidden Markov model based upon a conserved 57‐residue region in the loop between transmembrane segments 5 and 6. The hidden Markov model was also used to search the approximately one million… 

Isolation and Characterization of a Conserved Domain in the Eremophyte H+-PPase Family

This regular structure of these novel H+-PPases could provide important evidence for the evolutionary origin and study of the relationship between the structure and function among members of the H-PPase family.

Presence of a plant-like proton-translocating pyrophosphatase in a scuticociliate parasite and its role as a possible drug target

The molecular cloning and functional characterization of a gene encoding an H+-pyrophosphatase in the protozoan scuticociliate parasite Philasterides dicentrarchi, which infects turbot is described for the first time.

Polyphosphate-Peptide Synergy and the Organic Takeover at the Emergence of Life

Oligopeptides and pyro/triphosphates are potentially synergistic as they encourage each other’s synthesis, which would have been a key feature of this early stage in evolution before the advent of the ribosome.

The Structure and Catalytic Cycle of a Sodium-Pumping Pyrophosphatase

The structure of the sodium pumping M-PPase from Thermotoga maritima in the resting state reveals a previously unknown solution for ion pumping and reveals the conformational changes that are likely to accompany pyrophosphate binding and provide insight into the ion-pumping mechanism.

Pyrophosphate-Fueled Na+ and H+ Transport in Prokaryotes

The determination of the three-dimensional structures of H+- and Na+-pyrophosphatases has been another recent breakthrough in the studies of these cation pumps.

Structural Studies of Membrane-Bound Pyrophosphatases

The aim of this study was to solve the structure of a membrane-bound pyrophosphatase using Na2WO4 and tri-metyl lead acetate as a source and to find a suitable target protein for X-ray crystallography.

The Relevance of Peptides That Bind FeS Clusters, Phosphate Groups, Cations or Anions for Prebiotic Evolution

If di- or triphosphates were the major sources of instant energy in the earliest forms of metabolism, phosphate-binding nests can be said to have retained the structure required for energy generation and thus be one of the most ancient molecular relics in existence.

Characterization of protein families , sequence patterns , and functional annotations in large data sets

Two protein families were bioinformatically characterized the membrane associated proteins in eicosanoid and glutathione metabolism (MAPEG) and the Tripartite motif (TRIM) protein families and the complementarity of these two ontologies was demonstrated.

Functional Capabilities of the Earliest Peptides and the Emergence of Life

An objective of the present work is to demonstrate that sequence-independent peptides, or peptides with variable and unreliable lengths and sequences, have the potential to perform a variety of chemically useful functions such as anion and cation binding and membrane and channel formation as well as simple types of catalysis.

Functional capabilities of the earliest peptides and the emergence of life.

An objective of the present work is to demonstrate that sequence-independent peptides, or peptides with variable and unreliable lengths and sequences, have the potential to perform a variety of chemically useful functions such as anion and cation binding and membrane and channel formation as well as simple types of catalysis.



Membrane Topology of the H+-pyrophosphatase of Streptomyces coelicolor Determined by Cysteine-scanning Mutagenesis*

It is proposed that the basic structure of H+-PPases has 16 transmembrane domains with several large cytoplasmic loops containing functional motifs.

Mutagenic Analysis of Functional Residues in Putative Substrate-binding Site and Acidic Domains of Vacuolar H+-Pyrophosphatase*

Results suggest that the second acidic region is also implicated in the substrate hydrolysis and that at least two residues, Lys261and Glu263, are essential for the substrate-binding function.

An Unusual, His-dependent Family I Pyrophosphatase from Mycobacterium tuberculosis*

The structural and functional characterization of a unique family I PPase from Mycobacterium tuberculosis (mtPPase) that has two His residues (His21 and His86) in the active site show that the His residues in mtPPase are not essential for catalysis, although they determine cofactor specificity.

A Lysine Substitute for K+

It is demonstrated that a A460K substitution in C. hydrogenoformans H+-PPase is sufficient to confer K+ independence to both PPihydrolysis and PPi-energized H+ translocation, and a A463T mutation does not affect the K+dependence of H+, in conjunction with phylogenetic analyses.

Vacuolar H(+)-pyrophosphatase.

  • M. Maeshima
  • Biology, Chemistry
    Biochimica et biophysica acta
  • 2000

AVP2, a sequence-divergent, K(+)-insensitive H(+)-translocating inorganic pyrophosphatase from Arabidopsis.

The molecular and biochemical characterization of AVP2 is described, a sequence-divergent (36% identical) K(+)-insensitive, Ca(2+)-hypersensitive V-PPase active in both inorganic pyrophosphate hydrolysis and H(+) translocation, providing the first indication that plant V- PPases from the same organism fall into two distinct categories.

Tetra- and Nonapeptidyl Motifs in the Origin and Evolution of Photosynthetic Bioenergy Conversion

The first tentative model of the active site has resulted in a structure, which may be useful for attempts to extrapolate back to the hither toelusive molecular origin and evolution of the metabolism of phosphate compounds, specially those, which are directly involved in bioenergy conversion.

Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments.

It was found that a 34-residue helix-loop-helix peptide represents about 60% of the binding affinity found in the intact protein, and conservation of certain residues can vary in similar sites in similar proteins.