An immunochemical study of <i>Neurospora</i> nucleases

Fraser, Murray; Chow, Terry Y.-K.; Cohen, Helga J.; Koa, Helena

doi:10.1139/o86-018

Cited by 41 publications

(29 citation statements)

References 4 publications

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“…Several extracellular phosphatases have been characterized, including the PHO-3 repressible acid phosphatase and the PHO-2 repressible alkaline phosphatase. Two secreted phosphate-repressible alkaline DNases have been described (394), as well as a DNase A and a singlestrand-specific endonuclease (250). There are more than 30 nucleases and phosphatases in the Neurospora genome.…”

Section: Extracellular Digestionmentioning

confidence: 99%

Lessons from the Genome Sequence ofNeurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism

Borkovich

Alex

Yarden

et al. 2004

Microbiol Mol Biol Rev

598

618

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We present an analysis of over 1,100 of the ∼10,000 predicted proteins encoded by the genome sequence of the filamentous fungus Neurospora crassa. Seven major areas of Neurospora genomics and biology are covered. First, the basic features of the genome, including the automated assembly, gene calls, and global gene analyses are summarized. The second section covers components of the centromere and kinetochore complexes, chromatin assembly and modification, and transcription and translation initiation factors. The third area discusses genome defense mechanisms, including repeat induced point mutation, quelling and meiotic silencing, and DNA repair and recombination. In the fourth section, topics relevant to metabolism and transport include extracellular digestion; membrane transporters; aspects of carbon, sulfur, nitrogen, and lipid metabolism; the mitochondrion and energy metabolism; the proteasome; and protein glycosylation, secretion, and endocytosis. Environmental sensing is the focus of the fifth section with a treatment of two-component systems; GTP-binding proteins; mitogen-activated protein, p21-activated, and germinal center kinases; calcium signaling; protein phosphatases; photobiology; circadian rhythms; and heat shock and stress responses. The sixth area of analysis is growth and development; it encompasses cell wall synthesis, proteins important for hyphal polarity, cytoskeletal components, the cyclin/cyclin-dependent kinase machinery, macroconidiation, meiosis, and the sexual cycle. The seventh section covers topics relevant to animal and plant pathogenesis and human disease. The results demonstrate that a large proportion of Neurospora genes do not have homologues in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. The group of unshared genes includes potential new targets for antifungals as well as loci implicated in human and plant physiology and disease

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Section: Extracellular Digestionmentioning

confidence: 99%

Lessons from the Genome Sequence ofNeurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism

Borkovich

Alex

Yarden

et al. 2004

Microbiol Mol Biol Rev

598

618

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“…From mitochondria, a strand non-speci¢c endonuclease [11] and a ssDNA binding endo^exonuclease not inhibited by ATP [24] have also been isolated. Fraser et al [93] demonstrated by immunochemical techniques that all the above enzymes from N. crassa are derived from one or more related large inactive (precursor) polypeptides which undergo proteolysis to produce various active forms of nucleases. This inactive precursor was shown to have a M r of 93^95 kDa [94].…”

Section: Puri¢cationmentioning

confidence: 99%

“…This inactive precursor was shown to have a M r of 93^95 kDa [94]. Additionally, Fraser et al [93] showed that endo^exonucleases from A. nidulans and S. cerevisiae are immunologically related to N. crassa endoê xonuclease but not to single-strand-speci¢c nucleases like S1, P1 and mung bean nuclease. Similarly, isoforms of the nucleases were observed in S. aureus [95], B. subtilis [25], A. espejiana [12], S. marcescens kums 3958 [23], tobacco pollen [43], P. hybrida pollen [45] and S. marcescens [969 8].…”

Section: Puri¢cationmentioning

confidence: 99%

Sugar non-specific endonucleases

Rangarajan¹

2001

FEMS Microbiology Reviews

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Sugar non-specific endonucleases are multifunctional enzymes and are widespread in distribution. Apart from nutrition, they have also been implicated in cellular functions like replication, recombination and repair. Their ability to recognize different DNA structures has also been exploited for the determination of nucleic acid structure. Although more than 30 non-specific endonucleases have been isolated to date, very little information is available regarding their structure^function correlations except that of staphylococcal and Serratia nucleases. However, during the past few years, the primary structure, nature of the active site based on sequence homology, and the probable mechanism of action have been postulated for some of the enzymes. This review describes the purification, characteristics, biological role and applications of sugar non-specific endonucleases. ß

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“…The antibodies raised previously to the purified Neurospora endo-exonuclease were shown to cross-react not only with the nuclear and mitochondrial endo-exonuclease of S. cerevisiae described above but also with an intracellular endo-exonuclease of Aspergillus nidulans (H. Koa, M. J. Fraser, and E. Kafer, unpublished observations) and with a mitochondrial nuclease of mouse plasmacytoma cells (18). However, no immunochemical cross-reaction was seen with other fungal and plant nucleases with sugar-nonspecific but single-strand-specific endonuclease activities, such as the Si nuclease of Aspergilluls oryzae, the P1 nuclease of Penicillium citrinum, and mung bean nuclease, and also not with a number of DNases tested (11). Thus, the nuclear and mitochondrial sugar-nonspecific endo-exonuclease in eucaryotes may constitute a separate class of nucleases.…”

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confidence: 97%

Neurospora endo-exonuclease is immunochemically related to the recC gene product of Escherichia coli

1990

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Immunochemical cross-reaction between the endo-exonuclease of Neurospora crassa, an enzyme previously implicated in recombination and recombinational DNA repair, and the recC-encoded polypeptide of Esherichia coli has been detected by immunoblotting extracts of strains of E. coli having a deletion that includes the recBCD genes but carrying multicopy plasmids bearing all three of the recBCD genes or only one or two of these genes. It was predicted that homology would also be found at the amino acid sequence level between the recC polypeptide and both nuclear and mitochondrial endo-exonucleases of Saccharomyces cerevisiae, which cross-react with antibodies raised to the N. crassa endo-exonuclease. Since the gene for the S. cerevisiae mitochondrial enzyme, NUCI, has been cloned and sequenced and the predicted amino acid sequence is known, this sequence was aligned with the predicted amino acid sequence of the recC polypeptide. Extensive homology was found by aligning 306 of the 329 amino acids of the yeast mitochondrial nuclease sequence with the carboxy-terminal one-quarter of the amino acid sequence of the recC polypeptide.Possible roles for endo-exonuclease of Neurospora crassa in recombination and recombinational repair of nuclear and mitochondrial DNAs have been proposed previously, on the basis of strong similarities in the enzymic activities of this enzyme and those of the recBCD-encoded nuclease (exonuclease V) of Escherichia coli (4) and deficiencies in active endo-exonuclease in nuclei and mitochondria of the mutagen-sensitive uvs-3 mutant of Neurospora sp., which may be abnormal in recombination (12,15). In addition, an immunochemically related nuclear endo-exonuclease of 72 kilodaltons (kDa) was shown to be very deficient in the recombination and recombinational double-strand DNA break repair-deficient rad52 mutant of Saccharomyces cerevisiae (5, 6). The nuclear endo-exonuclease is encoded by an essential gene which has been cloned and is currently being sequenced (T. Y.-K. Chow, unpublished observations). A second endo-exonuclease, of 38 kDa, which is also immunochemically related to the N. crassa endo-exonuclease is present in the S. cerevisiae mitochondria (7). It is encoded by the nonessential NUCI gene, which has recently been cloned and sequenced (19).In contrast to E. coli exonuclease V, the N. crassa endo-exonuclease is sugar nonspecific, acting on both DNA and RNA, and although it is not ATP dependent or ATP stimulated in its actions, it does possess a distributive single-stranded DNA-specific endonuclease activity and a highly processive exonuclease activity with linear doublestranded DNA, like exonuclease V (4). The latter activity in vitro can generate long single-stranded tails and long gaps in duplex DNA, which would be potentially recombinogenic substrates if also generated in vivo. Under slightly different conditions in vitro, N. crassa endo-exonuclease has been shown recently to make site-specific single-and doublestrand breaks in linear, but not in covalently closed circular, V (17)....

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An immunochemical study of Neurospora nucleases

Cited by 41 publications

References 4 publications

Lessons from the Genome Sequence ofNeurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism

Lessons from the Genome Sequence ofNeurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism

Sugar non-specific endonucleases

Neurospora endo-exonuclease is immunochemically related to the recC gene product of Escherichia coli

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