Properties of thiamin‐binding proteins from sesame seed 2S albumins

“…The three STBPs differ in their molecular mass, affinity for thiamin and thiamin‐related compounds and isoelectric point. They resemble each other, however, in amino acid composition and the optimal pH for thiamin‐binding activity (Shimizu et al 1995; Watanabe et al 1999). In addition, the amino acid sequences of the small polypeptides of STBPs have been identified and are the same.…”

Section: Introductionmentioning

confidence: 98%

“…In addition, the amino acid sequences of the small polypeptides of STBPs have been identified and are the same. The N‐terminals of the large polypeptides of STBPs are blocked (Watanabe et al 1999). These results suggest that the STBPs are isomers.…”

Section: Introductionmentioning

confidence: 99%

Cloning and sequence analysis of cDNA encoding thiamin‐binding proteins from sesame seeds

Watanabe

Takahashi

Mitsunaga

2001

Physiologia Plantarum

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The amino acid sequences of the large polypeptides of thiamin-binding proteins (TBPs) from sesame (Sesamum indicum L.) seeds (STBP-I, -II and -III) were analyzed. The large polypeptides of STBP-I, -II and -III had the same amino acid sequences as did their small polypeptides. The peptide sequence information obtained from STBPs was used to synthesize DNA primers for amplification of the gene(s) encoding STBPs. A 200-bp fragment was amplified from cDNA synthesized from RNA from sesame seeds 4 weeks after flowering. The 200-bp fragment was used to clone full-length cDNA(s) encoding STBP(s) with RACE techniques. A 644-bp fragment was amplified, cloned and sequenced. The cDNA was a full-length clone encoding STBP(s). It contained an open reading frame, which defined a 143-residue polypeptide. The identified small and large polypeptide sequences of STBPs exactly matched the sequence encoded within the cDNA clone. These results indicated that the small and large polypeptides of STBPs were encoded on the mRNA as a single large proprotein precursor and that the final mature forms were generated by post-translational processing in the same manner as the other 2S albumins of plant seeds.

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“…On the other hand, the molecular masses of STBP-I, and -II are the same. They are composed of two 8.9-kDa subunits and their amino acid sequences are the same (Shimizu et al 1995;Watanabe et al 1999). The molecular mass of STBP-III is higher than that of STBP-I, and -II.…”

Section: Short Communicationmentioning

confidence: 99%

“…The molecular mass of STBP-III is higher than that of STBP-I, and -II. STBP-III is composed of two 9.3-kDa subunits and the amino acid sequence is identical to that of STBP-I and -II, except for the C-terminus of large polypeptide resulting in the difference of molecular mass (Shimizu et al 1995;Watanabe et al 1999). Consequently, STBP-I and -III differ from one another in Kd, Bmax, and molecular structure.…”

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Biosynthesis of thiamin-binding proteins in developing sesame seeds

Ampo

Asada

Takebayashi

et al. 2007

Plant Biotechnology

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Thiamin-binding proteins (TBPs) occur in many kinds of plant seeds. TBPs retain thiamin in dormant seeds and supply it for germ growth during germination. It is assumed that thiamin-TBP complex is a storage form of thiamin in the seeds and thiamin is converted to thiamin pyrophosphate during germination (Mitsunaga et al. 1987). The biochemical, structural and functional properties of the TBPs are well known (Shimizu et al. 1995;Watanabe 1999;Rapala-Kozik and Kozik 1999;Adachi et al. 2000;Adamek-Swierczynska and Kozik 2002;Watanabe et al. 2003Watanabe et al. , 2004Golda et al. 2004). Many of TBPs isolated from plant seeds are globulin proteins with molecular masses over 100 kDa; however, TBPs classified into albumin proteins, with smaller molecular masses, have been found in sesame seeds (Shimizu et al. 1995) and pea seeds (AdamekSwierczynska and Kozik 2002). Pea seeds had two TBPs: globulin TBP with a molecular mass of 150-170 kDa and albumin TBP with a molecular mass of 48 kDa, and sesame seeds had three albumin TBPs, termed STBP-I, -II and -III, with molecular masses of 17-19 kDa, whereas other plant seeds had only globulin TBP with a molecular mass over 100 kDa.The three STBPs resembled each other in molecular mass, molecular structure, and binding-activity to thiamin and thiamin-related compounds. STBP-I, and -II were composed of two 8.9-kDa subunits, respectively. STBP-III was composed of two 9.3-kDa subunits (Shimizu et al. 1995). STBP-II and -III bound one molecule of thiamin per molecule, and STBP-I bound 0.5 molecule (Shimizu et al. 1995). Moreover, the amino acid sequences of small polypeptides of the three STBPs were the same . The amino acid sequences of the large polypeptides were the same, except for the C-terminus of polypeptide chains resulting in differences in molecular mass between STBP-I, -II and -III. On the other hand, cDNA encoding STBPs was isolated and characterized (Watanabe et al. 2001). These results proposed the formation of STBP-I, -II and -III from the proprotein precursor by post-translational processing. However, it remains unclear whether the three STBPs are produced from the same large proprotein precursor or encoded by a gene family (Watanabe et al. 2001). In this paper, STBPs in developing sesame seeds were analyzed by column chromatography and SDS-PAGE. Furthermore, digested Abstract The formation of thiamin-binding proteins (TBPs) from sesame (Sesamum indicum L.) seeds (STBP-I, -II and -III) in developing seeds was investigated. Elution profiles of STBPs obtained from seeds at 4 to 6 weeks after flowering from the Q-Sepharose Fast Flow column showed that only one STBP was contained in the seeds at 4 weeks, and two STBPs were contained in the seeds at 5 weeks, and all three STBPs were contained in the seeds at 6 weeks as well as in mature seeds. SDS-PAGE of those STBPs demonstrated that STBP in the seeds at 4 weeks was large STBP termed as STBP-III, the molecular mass of which was higher than STBP-I and -II. In addition, it was demonstrated that small and large STBPs were co...

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Properties of thiamin‐binding proteins from sesame seed 2S albumins

Cited by 10 publications

References 11 publications

Accumulation and Degradation of Thiamin-binding Protein and Level of Thiamin in Wheat Seeds during Seed Maturation and Germination

Accumulation and Degradation of Thiamin-binding Protein and Level of Thiamin in Wheat Seeds during Seed Maturation and Germination

Cloning and sequence analysis of cDNA encoding thiamin‐binding proteins from sesame seeds

Biosynthesis of thiamin-binding proteins in developing sesame seeds

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