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Registro Completo |
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Biblioteca(s): |
Embrapa Meio Norte / UEP-Parnaíba. |
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Data corrente: |
20/09/1996 |
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Data da última atualização: |
16/10/2008 |
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Autoria: |
MIRKOV, T. E.; WAHLSTROM, J. M.; HAGIWARA, K.; FINARDI-FILHO, F.; KJEMTRUP, S.; CHRISPEELS, M. J. |
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Título: |
Evolutionary relationships among proteins in the phytohemagglutinin-arcelin-a-amylase inhibitor family of the common bean and its relatives. |
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Ano de publicação: |
1994 |
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Fonte/Imprenta: |
Plant Molecular Biology, v. 26, p. 1103-1113, 1994. |
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Idioma: |
Inglês |
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Conteúdo: |
The common bean, Phaseolus vulgaris, contains a family of defense proteins that comprises phytohemagglutinin (PHA), arcelim, and a-amylase inhibitor (aAI). Here we report eight new derived amino acid sequences of genes in this family obtained with either the polymerase chain reaction using genomic DNA, or by screening cDNA libraries made with RNA from developing beans. These new sequences are: two aAI sequences and arcelin-4 otained from a wild accession of P. vulgaris that is resistant to the Mexican bean weevil (Zabrotes subfasciatus) and the bean weevil (Acanthoscelides obtectus); an aAI sequence from the related species P. acutifolius (tepary bean); a PHA and an arcelin-like sequence from P. acutifolius; an aAI-like sequence from P. maculatus; and a PHA sequence from an arcelin-5 type P. vulgaris. A dendrogram of 16 sequences shows that they fall into the three identified groups: phytohemagglutinins, arcelins and aAIs. A comparison of these derived amino acid sequences indicates that one of the four amino acid residues that is conserved in all legume lectins and is required for carbohydrate binding is absent from all the arcelins; two of the four conserved residues needed for carbohydrate binding are missing from all the aAIs. Proteolytic processing at an Asn-Ser site is required for the activation of aAI, and this site is present in all aAI-like sequences; this processing site is also found at the same position in certain arcelins, which are not proteolytically processed. The presence of this site is therefore not sufficient for processing occur. MenosThe common bean, Phaseolus vulgaris, contains a family of defense proteins that comprises phytohemagglutinin (PHA), arcelim, and a-amylase inhibitor (aAI). Here we report eight new derived amino acid sequences of genes in this family obtained with either the polymerase chain reaction using genomic DNA, or by screening cDNA libraries made with RNA from developing beans. These new sequences are: two aAI sequences and arcelin-4 otained from a wild accession of P. vulgaris that is resistant to the Mexican bean weevil (Zabrotes subfasciatus) and the bean weevil (Acanthoscelides obtectus); an aAI sequence from the related species P. acutifolius (tepary bean); a PHA and an arcelin-like sequence from P. acutifolius; an aAI-like sequence from P. maculatus; and a PHA sequence from an arcelin-5 type P. vulgaris. A dendrogram of 16 sequences shows that they fall into the three identified groups: phytohemagglutinins, arcelins and aAIs. A comparison of these derived amino acid sequences indicates that one of the four amino acid residues that is conserved in all legume lectins and is required for carbohydrate binding is absent from all the arcelins; two of the four conserved residues needed for carbohydrate binding are missing from all the aAIs. Proteolytic processing at an Asn-Ser site is required for the activation of aAI, and this site is present in all aAI-like sequences; this processing site is also found at the same position in certain arcelins, which are not proteolytically process... Mostrar Tudo |
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Palavras-Chave: |
Amybase inhibitor; Arcelim; Argemina; Bean; Inibidor amibiase; Lectin. |
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Thesagro: |
Feijão; Lecitina. |
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Categoria do assunto: |
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Marc: |
LEADER 02362naa a2200277 a 4500
001 1078094
005 2008-10-16
008 1994 bl --- 0-- u #d
100 1 $aMIRKOV, T. E.
245 $aEvolutionary relationships among proteins in the phytohemagglutinin-arcelin-a-amylase inhibitor family of the common bean and its relatives.
260 $c1994
520 $aThe common bean, Phaseolus vulgaris, contains a family of defense proteins that comprises phytohemagglutinin (PHA), arcelim, and a-amylase inhibitor (aAI). Here we report eight new derived amino acid sequences of genes in this family obtained with either the polymerase chain reaction using genomic DNA, or by screening cDNA libraries made with RNA from developing beans. These new sequences are: two aAI sequences and arcelin-4 otained from a wild accession of P. vulgaris that is resistant to the Mexican bean weevil (Zabrotes subfasciatus) and the bean weevil (Acanthoscelides obtectus); an aAI sequence from the related species P. acutifolius (tepary bean); a PHA and an arcelin-like sequence from P. acutifolius; an aAI-like sequence from P. maculatus; and a PHA sequence from an arcelin-5 type P. vulgaris. A dendrogram of 16 sequences shows that they fall into the three identified groups: phytohemagglutinins, arcelins and aAIs. A comparison of these derived amino acid sequences indicates that one of the four amino acid residues that is conserved in all legume lectins and is required for carbohydrate binding is absent from all the arcelins; two of the four conserved residues needed for carbohydrate binding are missing from all the aAIs. Proteolytic processing at an Asn-Ser site is required for the activation of aAI, and this site is present in all aAI-like sequences; this processing site is also found at the same position in certain arcelins, which are not proteolytically processed. The presence of this site is therefore not sufficient for processing occur.
650 $aFeijão
650 $aLecitina
653 $aAmybase inhibitor
653 $aArcelim
653 $aArgemina
653 $aBean
653 $aInibidor amibiase
653 $aLectin
700 1 $aWAHLSTROM, J. M.
700 1 $aHAGIWARA, K.
700 1 $aFINARDI-FILHO, F.
700 1 $aKJEMTRUP, S.
700 1 $aCHRISPEELS, M. J.
773 $tPlant Molecular Biology$gv. 26, p. 1103-1113, 1994.
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Embrapa Meio Norte / UEP-Parnaíba (CPAMN-UEPP) |
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