Characterization of the subunits of β-conglycinin

Coates, J. B.; Medeiros, J.S.; Thanh, Vu Huu; Nielsen, Niels Chr.

doi:10.1016/0003-9861(85)90787-8

Cited by 101 publications

(80 citation statements)

References 28 publications

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“…1C. We determined that the DNA sequence produces an open reading frame with N-terminal amino acids similar to those present in the ,B-conglycinin p-subunit (4), that the CG4 gene contains five introns as predicted by the R-loop analysis, and that it differs from the CG-J a'-subunit gene (7) by the absence of a 0.56-kb insertion within the first exon.…”

Section: Methodsmentioning

confidence: 99%

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Cellular localization of soybean storage protein mRNA in transformed tobacco seeds

Barker

Harada

Goldberg

1988

Proc. Natl. Acad. Sci. U.S.A.

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We transformed tobacco plants with a soybean (3-conglycinin gene that encodes the 1.7-kilobase (3-subunit mRNA. We showed that the (8-conglycinin mRNA accumulates and decays during tobacco seed development and that (3-conglycinin mRNA is undetectable in the tobacco leaf. We utilized in situ hybridization to localize (8- Here, we introduced a p3-conglycinin 8-subunit gene into tobacco plants. Using in situ hybridization, we demonstrate that p-conglycinin mRNA is detectable only within the tobacco embryo and is localized preferentially within cotyledon and upper axis cells. In addition, we show that p-conglycinin mRNA is not detectable in the tobacco leaf, and that 8-conglycinin mRNA appears and disappears at precise stages of tobacco seed development. We conclude that sequences required for both temporal control and cell specificity are linked to the 8-subunit gene and that regulatory molecules that control 8-conglycinin gene expression are spatially distributed within analogous tobacco and soybean seed regions. MATERIALS AND METHODSIsolation of a j-Conglycinin Plasmid. The characteristics of the p-conglycinin cDNA plasmid A-16 have been described (5).DNA Isolation and Labeling. DNAs were isolated as described by Fischer and Goldberg (14) and were labeled by nick-translation (15).Polysomal mRNA Isolation. Soybean and tobacco polysomal mRNAs were isolated as described (16,17).Filter Hybridization Experiments. DNA gel-blot and RNA dot-blot experiments were carried out according to published procedures (18)(19)(20). RNA gel-blot studies were performed as described (5) except that nitrocellulose filters were used.In Situ Hybridization Experiments. In situ hybridization studies were carried out as described by Cox et al. (21) with modification. In brief, seeds 19 days after pollination (DAP) were fixed in 10% formalin/5% acetic acid/50% ethanol (22), embedded in paraffin, and sliced into 10-,um sections. Singlestranded p3-conglycinin 35S-labeled RNA probes were synthesized by using the pGEM transcription system (Promega Biotec). The 35S-labeled RNA probes were hydrolyzed to approximately 0.2 kb in size and then were hybridized with slides containing fixed seed sections for 14 hr at selection criteria of 420C, 0.3 M Na', and 50% formamide (21). A 35S-labeled anti-mRNA probe was used to localize pconglycinin mRNA within the tobacco seed while a 35s-labeled mRNA probe monitored nonspecific hybridization within the fixed seed section. Following hybridization, the fixed seed sections were incubated with RNase A at 50

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Section: Methodsmentioning

confidence: 99%

“…The major, 8-conglycinin polypeptides, designated a', a, and ,8 (3,4), are encoded by 2.5-kilobase (kb) (a'/a) and 1.7-kb (X3) mRNAs, respectively (5,6). P-Conglycinin mRNAs are highly homologous, differ primarily by the presence or absence of a 0.56-kb insertion sequence, and are transcribed from different genes (refs.…”

mentioning

confidence: 99%

Cellular localization of soybean storage protein mRNA in transformed tobacco seeds

Barker

Harada

Goldberg

1988

Proc. Natl. Acad. Sci. U.S.A.

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“…The sequence AATAAA is the highly conserved sequence which usually appears 10 -30 nucleotides upstream from the polyadenylation site of mRNAs [22,23]. This unique sequence was found at four places in the 3'-untrdnslated region of pCAN55-cDNA, and two of them are involved in the sequence AATAAATAAA which was also observed in cDNAs for pea legumin [23], soybean glycinin A5A4B3 precursor [24] and P-conglycinin [25].…”

Section: Nucleotide Sequence Of Cdna Clone For Canavalinmentioning

confidence: 99%

cDNAs for canavalin and concanavalin A from Canavalia gladiata seeds

Yamauchi¹,

Nakamura²,

Asahi³

et al. 1988

European Journal of Biochemistry

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By a method of Escherichia coli expression‐vector‐primed cDNA synthesis, a cDNA expression library was constructed from total poly(A)‐rich RNA that was prepared from immature embryos of Canavalia gladiata. Essentially full‐length cDNA clones for two seed proteins, canavalin and concanavalin A, were selected from the library by immunological screening of the colonies and in vitro RNA synthesis and translation. The complete amino acid sequence of canavalin was determined from the nucleotide sequence of the corresponding cDNA and was found to be very homologous to 7S seed proteins of other legumes. The nucleotide sequence of the cDNA predicts a 26‐amino‐acid extension in the precursor at the amino terminus of the mature canavalin. Canavalin mRNA and concanavalin A mRNA levels at successive stages of the seed development were estimated by RNA blot hybridization and results indicated that the two mRNA levels are differently regulated.

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“…The trimeric, 150-170 kDa, 7S protein is composed of a semi-random 4 association of the three subunits, a, a', and P (Derbyshire et al, 1976). Forms of the mature P-subunit contain, at most, one cys and no met among its approximately 416 amino acid residues (Thanh and Shibasaki, 1977;Coates et al, 1985). Tiemy et al (1987) reported the peptide sequence from one P-subunit gene containing no met or cys residues.…”

mentioning

confidence: 99%

Distribution and Mobilization of Sulfur during Soybean Reproduction

Naeve

Shibles

2005

Crop Science

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This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer.The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely aflFect reproduction.In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion.Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overiaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book.Photographs included in the original manuscript have been reproduced xerographically in this copy. Higher quality 6" x 9" black and white photographic prints are available for any photographs or illustrations appearing in this copy for an additional charge. Contact UMI directly to order. UMI GENERAL INTRODUCTION Dissertation OrganizationA discussion of results obtained from studies conducted on soybean sulfur metabolism is presented here as two manuscripts for the eventual submission for publication in Crop Science. A general introduction precedes these manuscripts giving a broad overview of plant sulfur metabolism, sulfur transpon, and soybean seed protein accumulation. A general conclusion chapter follows, summarizing findings of the two studies presented here.References cited in this dissertation are coalesced and listed at the end of the dissertation.The first manuscript paper discusses the distribution and mobilization of sulfur acquired by soybean during seed development, while the second takes up nitrogen and sulfur stress effects on mobilization of sulfur to developing soybean seed. RationaleSoybean seed is an important source of dietary protein for livestock and humans;however, soybean seed protein itself contains low, potentially growth-limiting concentrations of the sulfur-containing amino acids, methionine (met) and cysteine (cys), when used as the sole protein source for monogastric mammals. Methionine and cys are considered "essential amino acids" indicating that they cannot be synthesized de novo by monogastric mammals (Food and Agricultural Organization and World Health Organization, 1989). Methionine is the primary essential amino acid that is deficient in legume proteins (DeLumen et al., 1997), and soybean seed proteins contain about half of the met found in FAO's (Food and 2 Agricultural Organization) egg protein standard (Burton et al., 1982). This limitation reveals itself in high protein rations when the majority of the ingested protein is derived from soybean....

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Characterization of the subunits of β-conglycinin

Cited by 101 publications

References 28 publications

Cellular localization of soybean storage protein mRNA in transformed tobacco seeds

Cellular localization of soybean storage protein mRNA in transformed tobacco seeds

cDNAs for canavalin and concanavalin A from Canavalia gladiata seeds

Distribution and Mobilization of Sulfur during Soybean Reproduction

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