Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum

Yaoi, Takuro; Laksanalamai, Pongpan; Jiemjit, Anchalee; Kagawa, Hiromi; Alton, Thomas H.; Trent, Jonathan D.

doi:10.1006/bbrc.2000.3401

Cited by 11 publications

(4 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One of the corresponding products of the SDH reaction ( d ‐tagatose) is not reduced by Lad1 (data not shown), and the other one ( l ‐psicose) was unavailable for this study, but the two 3‐hexuloses are converted to galactitol and d ‐talitol, thus proving that their identification as products of the reaction is not an artefact. The occurrence of these two 3‐hexuloses in nature has so far not been reported, although the d ‐xylo‐3‐hexulose‐6‐phosphate is an intermediate in the autotrophic carbon dioxide metabolism in archaebacteria [26]. Reichert [27] reported that an l ‐glucitol dehydrogenase of a Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

The metabolic role and evolution of l‐arabinitol 4‐dehydrogenase of Hypocrea jecorina

Pail

Peterbauer

Schink

et al. 2004

European Journal of Biochemistry

View full text Add to dashboard Cite

L-Arabinitol 4-dehydrogenase (Lad1) of the cellulolytic and hemicellulolytic fungus Hypocrea jecorina (anamorph: Trichoderma reesei) has been implicated in the catabolism of L-arabinose, and genetic evidence also shows that it is involved in the catabolism of D-xylose in xylitol dehydrogenase (xdh1) mutants and of D-galactose in galactokinase (gal1) mutants of H. jecorina. In order to identify the substrate specificity of Lad1, we have recombinantly produced the enzyme in Escherichia coli and purified it to physical homogeneity. The resulting enzyme preparation catalyzed the oxidation of pentitols (L-arabinitol) and hexitols (D-allitol, D-sorbitol, L-iditol, L-mannitol) to the same corresponding ketoses as mammalian sorbitol dehydrogenase (SDH), albeit with different catalytic efficacies, showing highest k(cat)/K(m) for L-arabinitol. However, it oxidized galactitol and D-talitol at C4 exclusively, yielding L-xylo-3-hexulose and D-arabino-3-hexulose, respectively. Phylogenetic analysis of Lad1 showed that it is a member of a terminal clade of putative fungal arabinitol dehydrogenase orthologues which separated during evolution of SDHs. Juxtapositioning of the Lad1 3D structure over that of SDH revealed major amino acid exchanges at topologies flanking the binding pocket for d-sorbitol. A lad1 gene disruptant was almost unable to grow on L-arabinose, grew extremely weakly on L-arabinitol, D-talitol and galactitol, showed reduced growth on D-sorbitol and D-galactose and a slightly reduced growth on D-glucose. The weak growth on L-arabinitol was completely eliminated in a mutant in which the xdh1 gene had also been disrupted. These data show not only that Lad1 is indeed essential for the catabolism of L-arabinose, but also that it constitutes an essential step in the catabolism of several hexoses; this emphasizes the importance of such reductive pathways of catabolism in fungi.

show abstract

Section: Discussionmentioning

confidence: 99%

The metabolic role and evolution of l‐arabinitol 4‐dehydrogenase of Hypocrea jecorina

Pail

Peterbauer

Schink

et al. 2004

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Other thermophilic archaeal FtsZ proteins have also been investigated. One study isolated the ftsZ1 gene from the moderate thermophile Thermoplasma acidophilum [66]. Remarkably, expression of this gene in E. coli resulted in strong inhibition of cell division, which was attributed to interaction of the T. acidophilum FtsZ with the native FtsZ in E. coli and/or interference with its function.…”

Section: Biochemical Activities Of Archaeal Ftszmentioning

confidence: 99%

The Tubulin Superfamily in Archaea

Aylett

Duggin

2017

Subcellular Biochemistry

View full text Add to dashboard Cite

In comparison with bacteria and eukaryotes, the large and diverse group of microorganisms known as archaea possess a great diversity of cytoskeletal proteins, including members of the tubulin superfamily. Many species contain FtsZ, CetZ and even possible tubulins; however, some major taxonomic groups do not contain any member of the tubulin superfamily. Studies using the model archaeon, Halferax volcanii have recently been instrumental in defining the fundamental roles of FtsZ and CetZ in archaeal cell division and cell shape regulation. Structural studies of archaeal tubulin superfamily proteins provide a definitive contribution to the cytoskeletal field, showing which protein-types must have developed prior to the divergence of archaea and eukaryotes. Several regions of the globular core domain - the "signature" motifs - combine in the 3D structure of the common molecular fold to form the GTP-binding site. They are the most conserved sequence elements and provide the primary basis for identification of new superfamily members through homology searches. The currently well-characterised proteins also all share a common mechanism of GTP-dependent polymerisation, in which GTP molecules are sandwiched between successive subunits that are arranged in a head-to-tail manner. However, some poorly-characterised archaeal protein families retain only some of the signature motifs and are unlikely to be capable of dynamic polymerisation, since the promotion of depolymerisation by hydrolysis to GDP depends on contributions from both subunits that sandwich the nucleotide in the polymer.

show abstract

“…According to Yaoi et al, however, amino acid sequence analysis shows that regions I (ALDxxxxxxA) and II (VILxxDXKxxD) of OMPDC, which is involved in substrate recognition (pentose phosphates), are conserved in HPS. 23) KGPDC catalyzes the decarboxylation of 3-keto-Lgulonate 6-phosphate to L-xylulose 5-phosphate in the utilization of L-ascorbate. 24) KGDPC in several bacterial genomes are incorrectly annotated as ''probable hexulose phosphate synthases'' owing to their homology to HPS (30% identity).…”

Section: Reaction Mechanism Of Formaldehyde Fixation By Hpsmentioning

confidence: 99%

The Physiological Role of the Ribulose Monophosphate Pathway in Bacteria and Archaea

Kato

Yurimoto

Thauer

2006

Bioscience, Biotechnology, and Biochemistry

125

107

View full text Add to dashboard Cite

Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum

Cited by 11 publications

References 54 publications

The metabolic role and evolution of l‐arabinitol 4‐dehydrogenase of Hypocrea jecorina

The metabolic role and evolution of l‐arabinitol 4‐dehydrogenase of Hypocrea jecorina

The Tubulin Superfamily in Archaea

The Physiological Role of the Ribulose Monophosphate Pathway in Bacteria and Archaea

Contact Info

Product

Resources

About