Soybean sequence

Nagao, R.T., Czamecka, E., Gurley, W.B., Schoffl, F. Key, J.L. (1985). Genes for low-molecular-weight heat shock proteins of soybeans Sequence analysis of a multigene family. Molecular and Cellular Biology, 5, 3417-28. 

Huggins DR, Clapp CE, Allmaras RR, Lamb JA, Layese MF (1998) Carbon dynamics in corn-soybean sequences as estimated from natural carbon-13 abundance. Soil Sci Soc Am J 62 195-203... 

In order to establish a molecular data base for BR and begin to address questions (a) and (b) above, we have examined whether BR affects the transcription of auxin-induced genes in elongating soybean epicotyl sections using available auxin-induced soybean sequences as probes. More generally, we have shown changes in protein synthesis caused by BR in soybean epicotyls and hypocotyls by in vitro translation of mRNA (+ or - BR) followed by 2-D gel electrophoresis. 

Hagen, G., Uhrhammer, N., Guilfoyle, T.J. 1988. Regulation of expression of an auxin-induced soybean sequence by cadmium. J. Biol.Chem. 263 6442-6446. 

Schoffl, F., Raschke, E. Nagao, R.T. (1984). The DNA sequence analysis of soybean heat-shock genes and identification of possible regulatory promoter elements. EMBO Journal, 3, 2491-7. 

The peptide sequences obtained for codeinone reductase aligned well with the amino acid sequences for 6 -deoxychalcone synthase (chalcone reductase) from alfalfa, Glycerrhiza, and soybean. Knowledge of the relative positions of the peptides allowed for a quick RT-PCR based isolation of cDNAs encoding codeinone reductase from P. somniferum. The codeinone reductase isoforms are 53 % identical to chalcone reductase from soybean.25 By sequence comparison, both codeinone reductase and chalcone reductase belong to the aldo/keto reductase family, a group of structurally and functionally related NADPH-dependent oxidoreductases, and thereby possibly arise from primary metabolism. Six alleles encoding codeinone... 

Purple acid phosphatase (PAP) or tartrate-resistant phosphatase is not thought to be a protein phosphatase but it has a very similar dimetallic active site structure to that found in protein phosphatases. PAPs have been identified in bacteria, plants, mammals, and fungi. The molecular weights (animal 35 kDa, plant 55 kDa) are different and they exhibit low sequence homology between kingdoms but the residues involved in coordination of the metal ions are invariant. " There has been considerable debate as to the identity of the metal ions in PAPs in vivo. Sweet potato, Ipomoea batatas, has been shown to possess two different PAP enzymes and the active site of one of them has been shown to contain one Fe and one Zn " " ion. Another report has established that the active site of a PAP from sweet potato contains one Fe " and one Mn +. The well-characterized red kidney bean enzyme and the soybean enzyme contain Fe " and Zn. Claims that PAP from sweet potato has 2Fe ions or 2Mn ions have been discussed elsewhere. One explanation is that these are different forms of the enzyme, another is that because the metal ions are labile and are rapidly incorporated into the active site, the enzyme contains a mixture of metal ions in vivo and the form isolated depends on the conditions of isolation. 

It may also be surprising how easily this racemization may occur. Friedman and Liardon (126) studied the racemization kinetics for various amino acid residues in alkali-treated soybean proteins. They report that the racemization of serine, when exposed to 0.1M NaOH at 75°C, is nearly complete after just 60 minutes. However, caution must be used when examining apparent racemization rates for protein-bound amino acids. Liardon et al. (127) have also reported that the classic acid hydrolysis, employed to liberate constituent amino acids, causes amino acids to racemize to various degrees. This will necessarily result in D-isomer determinations that are biased high. Widely applicable correction factors are not possible since the racemization behavior of free amino acids is different from that of amino acid residues in proteins (which can be further affected by sequence). Of course, this is not a problem for free amino acid isomer determinations since the acid hydrolysis is unnecessary. Liardon et al. also describe an isotopic labeling/mass spectrometric method for determining true racemization rates unbiased by the acid hydrolysis. For an extensive and excellent review of the nutritional implications of the racemization of amino acids in foods, the reader is directed to a review article written by Man and Bada (128). 

The reduction of />coumaroyl-CoA (3.31) to />coumaryl aldehyde (3.69) is catalyzed by the enzyme cinnamoyl-CoA NADP oxidoreductase (CCR). This enzyme was initially purified from soybean cultures (Wegenmayer et al., 1976), and was later on efficiently isolated from lignifying cambium of eucalyps (Eucalyptus gunnii) (Gofifiier et al., 1994). A CCR cDNA was identified in a cDNA library that was screened with oligonucleotiede derived from the peptide sequence of the CCR protein. CCR is considered the first enzyme committed towards the biosynthesis of monolignols and shows... 

Fuller, F., Kunstrer, P.W., Nguyen, T. Verma, D.P.S. (1983). Soybean nodulin genes Analysis of cDNA clones reveals several major tissue-specific sequences in nitrogen-fixing root nodules. Proceedings of the National Academy of Sciences (USA) 80, 2594-8. 

Nirunsuksiri, W. Sengupta-Gopalan, C. (1990). Characterization of a novel nodulin gene in soybean that shares sequence similarity to the gene for nodulin-24. Plant Molecular Biology 15, 835-49. 

Accessory sequences, upstream from HSEs containing soybean hs promoter regions, have a significant influence on the amplitude of gene expression (Baumann etal., 1987 Czarnecka et al., 1989). Little is known about the functional structures within these regions and the molecular mechanism that enhances hs gene expression. Other sequences, e.g. hs gene mRNA leader and trailer sequences, are also very important for... 

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