Nucleotide and derived amino acid sequence of a catalase cDNA isolated from rice immature seeds

Mori, Haruhide; Higo, Kenichi; Higo, Hiromi; Minobe, Yuzo; Matsui, Hirokazu; Chiba, Shuya

doi:10.1007/bf00019211

Cited by 26 publications

(23 citation statements)

References 7 publications

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“…These included catalases from E. coli (54), Bacillus firmus (42), Bacillus subtilis (7), Oryza sativa (35), humans (41), and mouse (48). Loewen (27) mapped a locus which affects catalase 2 levels at this position and designated the locus katB.…”

Section: Resultsmentioning

confidence: 99%

“…3. Alignment of the heme-binding region of the katE gene product of B. subtilis (Bs2) with sequences of other catalases, namely HPII of E. coli (Ec) (54), the katA gene product of B. firmus (Bf) (42), catalase 1 of B. subtilis (Bs1) (7), catalase of Oryza sativa (Os) (35), catalase of mouse (Mm) (48), and human catalase (Hs) (41). The putative heme-binding region is printed in boldface type.…”

Section: Discussionmentioning

confidence: 99%

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Cloning, nucleotide sequence, and regulation of katE encoding a sigma B-dependent catalase in Bacillus subtilis

1995

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A B -dependent stress gene of Bacillus subtilis was localized downstream of the licS gene. The predicted amino acid sequence exhibited a significant similarity to the sequence of the katE-encoded catalase HPII of Escherichia coli, and we designated it the open reading frame katE. In a B. subtilis katE mutant, catalase 2 could not be detected. The amount of katE-specific mRNA was increased after heat, salt, or ethanol stress or after glucose starvation in a B -dependent manner. As in E. coli, the transcription of the katE gene in B. subtilis was unaffected by the addition of H 2 O 2 to exponentially growing cells. In contrast, the katA gene encoding catalase 1 of B. subtilis showed an induction pattern different from that of katE; katA expression was strongly increased by oxidative stress. The similarity between E. coli S -dependent genes and B. subtilis B -dependent genes suggests that both may confer multiple stress resistance to stationary-phase cells.In its natural environment Bacillus subtilis is often exposed to limiting amounts of nutrients and high salt concentrations as well as alterations in pH and temperature. As a consequence, B. subtilis is well equipped with a stress defense machinery to cope with these growth-restricting conditions. The very strong induction of a typical set of proteins in B. subtilis, which we call general stress proteins, occurs within the first minutes after the exposure of cells to stress (21,22,44,53) and is therefore one of the earliest responses to environmental changes.The alternative sigma factor B , which is one of 10 sigma factors in B. subtilis identified so far (33), appears to be an important regulator of the synthesis of stress-induced proteins (10,52,53). The increased activity of B after stress or early in stationary phase has been correlated with the increased synthesis of B -dependent stress proteins (5, 9-11, 53). In a sigB deletion mutant these proteins fail to be induced. Nevertheless, the mutation of sigB did not result in an increased sensitivity to stress or starvation. Therefore, the physiological role of B under these conditions remains obscure (17).In order to understand the role of B , it is necessary to investigate the function and regulation of genes controlled by sigB in more detail. ctc (20), csbA (12), and sigB (9, 10, 25) were the first genes shown to be subject to B -dependent regulation. Both ctc and sigB are strongly induced upon entry into stationary phase and after heat, salt, or ethanol stress (4, 9, 53). Recently, we have shown that the gsiB gene, which was originally identified as a gene induced by glucose starvation (37), belongs to the general stress genes in B. subtilis and requires B for its induction in response to various stimuli (32, 53). Unfortunately, the physiological functions of the gene products of csbA, ctc, and gsiB have not yet been identified.Recently, new csb loci have been identified by a genetic approach (10). The expression of these csb loci is either completely or partially dependent on B . One of these loci is gtaB (...

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cloning, nucleotide sequence, and regulation of katE encoding a sigma B-dependent catalase in Bacillus subtilis

1995

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“…A PTS 1 sequence is found 9 amino acids from the carboxyl terminus in all known plant catalases, which the exception of catalases from rice [99], castor bean (CAT1) [ 147], cotton (SU 1) [ 100], and the mitochondrial CAT-3 from maize [ 118]. Yet, the functionality of these sequences in peroxisomal targeting has thus far not been evidenced.…”

Section: Subcellular Distribution and Targetingmentioning

confidence: 95%

Catalases in plants

et al. 1995

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“…Two cDNA clones of catalase genes (CatA and CatB) have been isolated from rice (Mori et al, 1992;Morita et al, 1994). The difference in SA sensitivity of catalase activity from different rice tissues prompted us to utilize these cloned genes to analyze (a) the size of the catalase gene family, (b) the spatial expression of catalase genes, and (c) the primary structures of catalase proteins in rice.…”

Section: Catalase Gene Organizationmentioning

confidence: 99%

Differential Accumulation of Salicylic Acid and Salicylic Acid-Sensitive Catalase in Different Rice Tissues

et al. 1997

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We previously proposed that salicylic acid (SA)-sensitive catalases serve as biological targets of SA in plant defense responses. To further examine the role of SA-sensitive catalases, we have analyzed the relationship between SA levels and SA sensitivity of catalases in different rice (Oryza saliva) tissues. We show here that, whereas rice shoots contain extremely high levels of free SA, as previously reported ( , rice roots and cell-suspension cultures have very low SA levels. Catalases from different rice tissues also exhibit differences in sensitivity to SA. Catalase from rice shoots is insensitive to SA, but roots and cell-suspension cultures contain SA-sensitive catalase. The difference in SA sensitivity of catalases from these different tissues correlates with the tissue-specific expression of two catalase genes, CafA and CafB, which encode highly distinctive catalase proteins. CafA, which encodes a catalase with relatively low sequence homology to the tobacco SA-sensitive catalases, is expressed at high levels exclusively in the shoots. On the other hand, in roots and cell-suspension cultures, with northern analysis we detected expression of only the CafB gene, which encodes a catalase with higher sequence homology to tobacco catalases. The role of catalases in mediating some of the SA-induced responses is discussed in light of these results and the recently defined mechanisms of catalase inhibition by SA.

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Nucleotide and derived amino acid sequence of a catalase cDNA isolated from rice immature seeds

Cited by 26 publications

References 7 publications

Cloning, nucleotide sequence, and regulation of katE encoding a sigma B-dependent catalase in Bacillus subtilis

Cloning, nucleotide sequence, and regulation of katE encoding a sigma B-dependent catalase in Bacillus subtilis

Catalases in plants

Differential Accumulation of Salicylic Acid and Salicylic Acid-Sensitive Catalase in Different Rice Tissues

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