Solution structure of a BolA‐like protein from<i>Mus musculus</i>

Kasai, Takuma; Inoue, Makoto; Koshiba, S.; Yabuki, Takashi; Aoki, Masaaki; Nunokawa, Emi; Seki, Eiko; Matsuda, Takayoshi; Matsuda, Natsuko; Tomo, Yasuko; Shirouzu, Mikako; Terada, Takaho; Obayashi, Naomi; Hamana, H.; Shinya, Naoko; Tatsuguchi, Ayako; Yasuda, Satoko; Yoshida, Mayumi; Harada, Hiroshi; Matsuo, Yo; Tani, Kazuhide; Suzuki, Harukazu; Arakawa, Takahiro; Carninci, Piero; Kawai, Jun; Hayashizaki, Yoshihide; Kigawa, T.; Yokoyama, Shigeyuki

doi:10.1110/ps.03401004

Cited by 48 publications

(71 citation statements)

References 29 publications

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“…The molecular function of BolA is unknown and using sequence-to-profile searches (PSI-Blast) [13], we could not detect homology of BolA to sequences with a known molecular function. Recently, however, the 3D structure of a Mus musculus member of the BolA family has been published [7]. According to the Dali 3D structure classification system, BolA is homologous to OsmC (Table 1).…”

Section: Bola Is Homologous To the Peroxide Reductase Osmcmentioning

confidence: 99%

“…BolA and the N-terminal domain of OsmC have a class II KH fold. They distinguish themselves from other members of this fold because they both miss the GxxG element [7], which otherwise is well conserved in the class II KH fold and which appears essential …”

Section: Bola Is Homologous To the Peroxide Reductase Osmcmentioning

confidence: 99%

“…The structures, BolA of M. musculus (1v9j) and OsmC of E. coli (1ml8), were aligned with SHEBA [36]. Indicated are the a1, a2, a3 helix and the 3 10 helix of BolA, the nomenclature is adapted from Kasai et al [7]. The main difference between the structures is that the a3 helix of OsmC is one turn longer than the one of BolA.…”

Section: Bola Is Homologous To the Peroxide Reductase Osmcmentioning

confidence: 99%

“…Bola has therewith been proposed to be a regulator of cell wall biosynthetic enzymes [6]. Recently, the structure of the BolA homolog in Mus musculus has been determined [7]. BolA has a class II KH fold, instances of which are known to bind DNA and RNA and therewith support a regulatory role for BolA.…”

Section: Introductionmentioning

confidence: 99%

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Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin

et al. 2004

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Genomes, functional genomics data and 3D structure reflect different aspects of protein function. Here, we combine these data to predict that BolA, a widely distributed protein family with unknown function, is a reductase that interacts with a glutaredoxin. Comparisons at the 3D structure level as well as at the sequence profile level indicate homology between BolA and OsmC, an enzyme that reduces organic peroxides. Complementary to this, comparative analyses of genomes and genomics data provide strong evidence of an interaction between BolA and the mono-thiol glutaredoxin family. The interaction between BolA and a mono-thiol glutaredoxin is of particular interest because BolA does not, in contrast to its homolog OsmC, have evolutionarily conserved cysteines to provide it with reducing equivalents. We propose that BolA uses the mono-thiol glutaredoxin as the source for these.

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Section: Bola Is Homologous To the Peroxide Reductase Osmcmentioning

confidence: 99%

Section: Bola Is Homologous To the Peroxide Reductase Osmcmentioning

confidence: 99%

Section: Bola Is Homologous To the Peroxide Reductase Osmcmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin

et al. 2004

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“…In A. nidulans, SecC, a homolog of S. cerevisiae Sec3, accumulates at the plasma membrane anterior to the Spitzenkörper and may function as a landmark for secretion ( Taheri-Talesh et al, 2008). Moreover, a higher expression of TmelAip3, a polarisome component and of TmelBoi1A ( Kasai et al, 2004 andKnechtle et al, 2006) can reflect a higher rate of hyphal growth.…”

Section: Hyphal Growth Machinery and Its Transcriptional Regulationmentioning

confidence: 99%

Hyphal and cytoskeleton polarization in Tuber melanosporum: A genomic and cellular analysis

Amicucci

Balestrini

Kohler

et al. 2011

Fungal Genetics and Biology

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Filamentous polarized growth involves a series of events including polarization of the cytoskeleton to selected growth sites, and the transport of secretory vesicles containing the components required for growth. The availability of fungal genome sequences has recently led to the identification of a large number of proteins involved in these processes. We have explored the Tuber melanosporum genome sequence by searching for homologs of genes known to play crucial roles in the morphogenesis and cell polarity of yeasts and filamentous fungi. One hundred and forty-nine genes have been identified and functionally grouped according to the deduced amino acid sequences (44 genes involved in cell polarity/morphogenesis, 39 belonging to the actin cytoskeleton and 66 involved in membrane dynamics, septation and exocytosis). A detailed gene annotation has shown that most components of the cell polarity machinery, morphogenesis and cytoskeleton found in yeasts and filamentous fungi are conserved, although the degree of similarity varies from strong to weak. Microscopic analysis of quick-frozen truffle hyphae detected the characteristic subcellular components of the hyphal tip in septate filamentous fungi, while transcript profiles revealed a moderately variable pattern during the biological cycle.

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Green tea catechin extract in intervention of chronic breast cell carcinogenesis induced by environmental carcinogens

Rathore

Wang

2011

Molecular Carcinogenesis

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Sporadic breast cancers are mainly attributable to long-term exposure to environmental factors, via a multi-year, multi-step, and multi-path process of tumorigenesis involving cumulative genetic and epigenetic alterations in the chronic carcinogenesis of breast cells from a non-cancerous stage to precancerous and cancerous stages. Epidemiologic and experimental studies have suggested that green tea components may be used as preventive agents for breast cancer control. In our research, we have developed a cellular model that mimics breast cell carcinogenesis chronically induced by cumulative exposures to low doses of environmental carcinogens. In this study, we used our chronic carcinogenesis model as a target system to investigate the activity of green tea catechin extract (GTC) at non-cytotoxic levels in intervention of cellular carcinogenesis induced by cumulative exposures to pico-molar 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) and benzo[a]pyrene (B[a]P). We identified that GTC, at a non-cytotoxic, physiologically-achievable concentration of 2.5μg/mL, was effective in suppressing NNK- and B[a]P-induced cellular carcinogenesis, as measured by reduction of the acquired cancer-associated properties of reduced dependence on growth factors, anchorage-independent growth, increased cell mobility, and acinar-conformational disruption. We also detected that intervention of carcinogen-induced elevation of reactive oxygen species (ROS), increase of cell proliferation, activation of the ERK pathway, DNA damage, and changes in gene expression may account for the mechanisms of GTC's preventive activity. Thus, GTC may be used in dietary and chemoprevention of breast cell carcinogenesis associated with long-term exposure to low doses of environmental carcinogens.

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Solution structure of a BolA‐like protein fromMus musculus

Cited by 48 publications

References 29 publications

Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin

Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin

Hyphal and cytoskeleton polarization in Tuber melanosporum: A genomic and cellular analysis

Green tea catechin extract in intervention of chronic breast cell carcinogenesis induced by environmental carcinogens

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