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| 005 | 20250305143037.0 | ||
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| 022 | _a0176-1617 | ||
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_aMSU _bEnglish _cMSU _erda |
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| 050 | 0 | 0 | _aQK711.2 JOU |
| 100 | 1 |
_aPinedo, Marcela _eauthor |
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| 245 | 1 | 0 |
_aMolecular characterization of Helja, an extracellular jacalin-related protein from Helianthus annuus: Insights into the relationship of this protein with unconventionally secreted lectins _ccreated by Marcela Pinedo 1, Facundo Orts 2, André de Oliveira Carvalho 3, Mariana Regente 4, Julia Ribeiro Soares 5, Valdirene Moreira Gomes 6, Laura de la Canal 7 |
| 264 | 0 |
_aAmsterdam: _bElsevier GmbH, _c2015. |
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| 336 |
_2rdacontent _atext _btxt |
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| 337 |
_2rdamedia _aunmediated _bn |
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| 338 |
_2rdacarrier _avolume _bnc |
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| 440 |
_aJournal of plant physiology _vVolume 183 |
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| 520 | 3 | _aJacalin-related lectins (JRLs) encompass cytosolic, nuclear and vacuolar members displaying the jacalin domain in one or more copies or in combination with unrelated domains. Helianthus annuus jacalin (Helja) is a mannose-specific JRL previously identified in the apoplast of Helianthus annuus seedlings, and this protein has been proposed to follow unconventional secretion. Here, we describe the full-length Helja cDNA sequence, which presents a unique jacalin domain (merolectin) and the absence of a signal peptide, confirming that the protein cannot follow the classical ER-dependent secretory pathway. Helja mRNA is present in seeds, cotyledons, roots and hypocotyls, but no transcripts were detected in the leaves. Searches for sequence similarity showed that Helja is barely similar to other JRLs present in H. annuus databases and less than 45% identical to other monocot or dicot JRLs. Strikingly, most of the merolectins recovered through data mining using Helja as a query were predicted as apoplastic, although most of these proteins lack the signal peptide required for classical secretion. Thus, Helja is the first bait identified to recover putative unconventionally secreted lectins. Because the recovered JRLs are widely distributed among the plant kingdom, an as yet unknown role for jacalin lectins in the apoplast is emerging. | |
| 650 | _aApoplast | ||
| 650 | _aExtracellular proteins | ||
| 650 | _aJacalin domain | ||
| 700 | 1 |
_aOrts, Facundo _eco-author |
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| 700 | 1 |
_aCarvalho, André de Oliveira _eco-author |
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| 700 | 1 |
_aRegente, Mariana _eco-author |
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| 700 | 1 |
_aSoares, Julia Ribeiro _eco-author |
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| 700 | 1 |
_aGomes, Valdirene Moreira _eco-author |
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| 700 | 1 |
_aCanal, Laura de la _eco-author |
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| 856 | _uhttps://doi.org/10.1016/j.jplph.2015.06.004 | ||
| 942 |
_2lcc _cJA |
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| 999 |
_c169151 _d169151 |
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