Characterization of Gmhsp26-A, a stress gene encoding a divergent heat shock protein of soybean: heavy-metal-induced inhibition of intron processing.

We determined the DNA sequence and mapped the corresponding transcripts of a genomic clone containing the Gmhsp26-A gene of soybean. This gene is homologous to the previously characterized cDNA clone pCE54 (E. Czarnecka, L. Edelman, F. Schöffl, and J. L. Key, Plant Mol. Biol. 3:45-58, 1984) and is expressed in response to a wide variety of physiological stresses including heat shock (HS). S1 nuclease mapping of transcripts and a comparison of the cDNA sequence with the genomic sequence indicated the presence of a soybean seedlings with either CdCl2 or CuSO4. Analysis of the 5' termini of transcripts indicated the presence of one major and at least two minor start sites. In each case, initiation occurred 27 to 30 base pairs downstream from a TATA-like motif, and thus each initiation site appears to be promoted by the activity of a separate subpromoter. The three subpromoters are all associated with sequences showing low homology to the HS consensus element of Drosophila melanogaster HS genes and are differentially induced in response to various stresses. Within the carboxyl-terminal half of the protein, hydropathy analysis of the deduced amino acid sequence indicated a high degree of relatedness to the small HS proteins. A comparison of the primary amino acid sequence of hsp26-A with sequences of the small HS proteins suggested that this stress protein is highly diverged and may therefore be specialized for stress adaptation in soybean.

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Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases.

Genetics ◽

10.1093/genetics/131.3.531 ◽

1992 ◽

Vol 131 (3) ◽

pp. 531-539 ◽

Cited By ~ 6

Author(s):

C Bornaes ◽

J G Petersen ◽

S Holmberg

Keyword(s):

Saccharomyces Cerevisiae ◽

Amino Acid ◽

Amino Acid Sequence ◽

Transcription Initiation ◽

Open Reading Frame ◽

Predicted Amino Acid Sequence ◽

S1 Nuclease ◽

Reading Frame ◽

Threonine Dehydratase ◽

Nuclease Mapping

Abstract The catabolic L-serine (L-threonine) dehydratase of Saccharomyces cerevisiae allows the yeast to grow on media with L-serine or L-threonine as sole nitrogen source. Previously we have cloned the CHA1 gene by complementation of a mutant, cha1, lacking the dehydratase activity. Here we present the DNA sequence of a 1,766-bp fragment of the CHA1 region encompassing an open reading frame of 1080 bp. Comparison of the predicted amino acid sequence of the CHA1 polypeptide with that of other serine/threonine dehydratases revealed several blocks of sequence homology. Thus, the amino acid sequence of rat liver serine dehydratase (SDH2) and the CHA1 polypeptide are 44% homologous allowing for conservative substitutions, while 36% similarity is found between the catabolic threonine dehydratase (tdcB) of Escherichia coli and the CHA1 protein. This strongly suggests that CHA1 is the structural gene for the yeast catabolic serine (threonine) dehydratase. S1-nuclease mapping of the CHA1 mRNA ends showed a major transcription initiation site corresponding to an untranslated leader of about 19 nucleotides, while a major polyadenylation site was located about 86 nucleotides downstream from the open reading frame. Furthermore, we have mapped the chromosomal position of the CHA1 gene to less than 0.5 kb centromere proximal to HML on the left arm of chromosome III.

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Genomic organization and chromosomal localization of the mouse synexin gene

Biochemical Journal ◽

10.1042/bj3010835 ◽

1994 ◽

Vol 301 (3) ◽

pp. 835-845 ◽

Cited By ~ 3

Author(s):

Z Y Zhang-Keck ◽

M Srivastava ◽

C A Kozak ◽

H Caohuy ◽

A Shirvan ◽

...

Keyword(s):

Transcription Initiation ◽

Regulatory Elements ◽

Initiation Site ◽

Gene Encoding ◽

S1 Nuclease ◽

Mapping Sequence ◽

Mouse Tissues ◽

Potential Promoter ◽

Flanking Region ◽

Nuclease Mapping

We have isolated and characterized the gene encoding mouse synexin, which consists of 14 exons and spans approximately 30 kbp of genomic DNA. The protein's unique N-terminal domain is encoded by six exons, and the C-terminal tetrad repeat, the site of the membrane-fusion and ion-channel domain, is encoded by seven exons. The first exon encodes the 5′-untranslated region. Analysis of synexin-gene expression in different mouse tissues shows that mRNA with exon 6 is only present in brain, heart and skeletal muscle. mRNA lacking exon 6 is expressed in all tissues we have examined. The initiation site for transcription was determined by primer-extension analysis and S1 nuclease mapping. Sequence analysis of the 1.3 kb 5′-flanking region revealed that the promoter has a TATA box located at position -25 and a number of potential promoter and regulatory elements. A CCAAT motif was not observed but CCATT is located in an appropriate position for the CCAAT motif upstream from the transcription-initiation start site. In addition, the 5′-flanking region contains two sets of palindromic sequences. Finally, we have determined that the functional synexin gene (Anx7) is located on mouse chromosome 14 and that a pseudogene (Anx7-ps1) is located on chromosome 10.

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Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

Bioscience Biotechnology and Biochemistry ◽

10.1093/bbb/zbaa066 ◽

2020 ◽

Vol 85 (3) ◽

pp. 626-629

Author(s):

Hisashi Muramatsu ◽

Hiroki Maguchi ◽

Taisuke Harada ◽

Takehiro Kashiwagi ◽

Chul-Sa Kim ◽

...

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Propionic Acid ◽

Unknown Function ◽

Protein Family ◽

Amino Acid Sequence Analysis ◽

Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

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Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)98888-5 ◽

1991 ◽

Vol 266 (19) ◽

pp. 12242-12248 ◽

Cited By ~ 1

Author(s):

M. Vai ◽

E. Gatti ◽

E. Lacanà ◽

L. Popolo ◽

L. Alberghina

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Rich Region ◽

Gene Encoding

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cDNA Sequence and Deduced Amino Acid Sequence of a Fungal Stress Protein Induced inRhizopus nigricansby Steroids

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1998.9314 ◽

1998 ◽

Vol 250 (3) ◽

pp. 664-667 ◽

Cited By ~ 5

Author(s):

Bronislava Črešnar ◽

Andreja Plaper ◽

Katja Breskvar ◽

Tamara Hudnik-Plevnik

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Cdna Sequence ◽

Stress Protein

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Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

Journal of Bacteriology ◽

10.1128/jb.183.6.1954-1960.2001 ◽

2001 ◽

Vol 183 (6) ◽

pp. 1954-1960 ◽

Cited By ~ 12

Author(s):

Grit Zarnt ◽

Thomas Schräder ◽

Jan R. Andreesen

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Alcohol Dehydrogenase ◽

Tertiary Structure ◽

Ralstonia Eutropha ◽

Signal Sequence ◽

Substrate Inhibition ◽

Catalytic Efficiency ◽

Gene Encoding

ABSTRACT The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparentk cat/Km andK i values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k cat/Km value of 788 × 104 M−1 s−1. The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo (tfaA) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases.

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Purification and Partial Amino Acid Sequence of the Major 70,000-Dalton Heat Shock Protein in Neurospora crassa

Experimental Mycology ◽

10.1006/emyc.1993.1035 ◽

1993 ◽

Vol 17 (4) ◽

pp. 362-367 ◽

Cited By ~ 8

Author(s):

Franco Fracella ◽

Saadat Mohsenzadeh ◽

Ludger Rensing

Keyword(s):

Amino Acid ◽

Heat Shock ◽

Amino Acid Sequence ◽

Heat Shock Protein ◽

Neurospora Crassa ◽

Partial Amino Acid Sequence

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Purification of a mature form of 60kDa heat-shock protein (chaperonin homolog) from porcine kidney and its partial amino acid sequence

International Journal of Biochemistry ◽

10.1016/0020-711x(92)90079-g ◽

1992 ◽

Vol 24 (9) ◽

pp. 1507-1510 ◽

Cited By ~ 4

Author(s):

Wakui Hideki ◽

Itoh Hideaki ◽

Tashima Yohtalou ◽

Kobayashi Ryoji ◽

Nakamoto Yasushi ◽

...

Keyword(s):

Amino Acid ◽

Heat Shock ◽

Amino Acid Sequence ◽

Heat Shock Protein ◽

Porcine Kidney ◽

Partial Amino Acid Sequence ◽

Mature Form

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The EGD1 product, a yeast homolog of human BTF3, may be involved in GAL4 DNA binding.

Molecular and Cellular Biology ◽

10.1128/mcb.12.12.5683 ◽

1992 ◽

Vol 12 (12) ◽

pp. 5683-5689 ◽

Cited By ~ 29

Author(s):

M R Parthun ◽

D A Mangus ◽

J A Jaehning

Keyword(s):

Amino Acid ◽

Dna Binding ◽

Amino Acid Sequence ◽

Yeast Cells ◽

Stable Complex ◽

Affinity Column ◽

Gene Encoding ◽

Heat Stable ◽

Gel Retardation ◽

Final Purification Step

A variety of techniques, including filter binding, footprinting, and gel retardation, can be used to assay the transcriptional activator GAL4 (Gal4p) through the initial steps of its purification from yeast cells. Following DNA affinity chromatography, Gal4p still bound DNA selectively when assayed by filter binding or footprinting. However, the affinity-purified protein was no longer capable of forming a stable complex with DNA, as assayed by gel retardation. Mixing the purified Gal4p with the flowthrough fraction from the DNA affinity column restored gel retardation complex formation. Gel retardation assays were used to monitor the purification of a heat-stable Gal4p-DNA complex stabilization activity from the affinity column flowthrough. The activity coeluted from the final purification step with polypeptides of 21 and 27 kDa. The yeast gene encoding the 21-kDa protein was cloned on the basis of its N-terminal amino acid sequence. The gene, named EGD1 (enhancer of GAL4 DNA binding), encodes a highly basic protein (21% lysine and arginine) with a predicted molecular mass of 16.5 kDa. The amino acid sequence of the EGD1 product, Egd1p, is highly similar to that of the human protein BTF3 (X. M. Zheng, D. Black, P. Chambon, and J. M. Egly, Nature [London] 344:556-559, 1990). Although an egd1 null mutant was viable and Gal+, induction of the galactose-regulated genes in the egd1 mutant strain was significantly reduced when cells were shifted from glucose to galactose.

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