Abundant embryonic mRNA in field bean (Vicia faba L.) codes for a new class of seed proteins: cDNA cloning and characterization of the primary translation product

Abstract

cDNA clones have been constructed bearing inserts for a specific mRNA class of high abundance in developing seeds of field bean (Vicia faba L.). Three full-length clones representing transcripts of different genes were sequenced and conceptually translated into a M=30 000 primary gene product. The structural analysis of the derived amino acid sequence revealed distinct domains: (i) a cleavable signal peptide; (ii) a hydrophilic N-terminal stretch possessing two serine clusters; (iii) a valine cluster and a hydrophobic domain in the C-terminal part of the polypeptide. The amino acid sequence of the polypeptide does not show homology with other known proteins.The corresponding mRNA could be isolated using cDNA clones and was efficiently translated in various systems. In a cell-free system the presence of a functional signal peptide was shown, which interacts with the signal recognition particle resulting in a cotranslational translocation across the membrane of the endoplasmic reticulum. If synthesized in Xenopus oocytes the translation product of the mRNA was secreted out of the cell. Homologous mRNA was found to be present also in developing cotyledons of pea (Pisum sativum L.) and french bean (Phaseolus vulgaris L.).

Isolation and characterization of three families of auxin down-regulated cDNA clones

“…This combined with the fact that these clones seemed to have a strong secondary structure at the 5' end, based on repeated difficulty in sequencing through that region, suggests that in the case of both these clones, the reverse transcriptase stopped at a specific point having a particularly strong secondary structure. A search of the sequence data banks showed a 46~o homology to an unknown protein isolated from seeds of Vicia faba [ 19].…”

Genome-wide identification of BURP domain-containing genes in rice reveals a gene family with diverse structures and responses to abiotic stresses

“…So the most obvious region, including a short and nonrepetitive segment and an optional repeat segment, may be crucial for their distinct functions. But the short and nonrepetitive segment may be considered simply as a kind of stuVer fragment in BNM2 and VtUSP (Bassüner et al 1988). The region following the N-terminal signal peptide may have a delivery function to transport the proteins to a cellular target compartment; for instance, the cell wall for PG1 .…”

“…Many BURP domaincontaining proteins have been reported to be ubiquitous in plant species. Examples are BNM2, an oilseed rape (Brassica napus L.) microspore protein (Boutilier et al 1994;Treacy et al 1997); VfUSP, an unknown seed protein from faba bean (Vicia faba L.) (Bassüner et al 1988;Baumlein et al 1991); RD22, an Arabidopsis thaliana (L.) Heynh. dehydration-responsive protein (Yamaguchi-Shinozaki and Shinozaki 1993); PG1 , a -subunit of polygalacturonase isoenzyme 1 of tomato (Lycopersicon esculentum L.) (Zheng et al 1992;Watson et al 1994); ADR6, a soybean [Glycine max (L.) Merr.]…”

Molecular cloning and characterization of genes encoding BURP domain-containing protein in the mangrove, Bruguiera gymnorrhiza

“…Members of the BURP domain-containing protein family are widely distributed among ubiquitous plant species, for example, ADR6 from Glycine max (Datta et al 1993), Zrp2 from Zea mays (Held et al 1997), an unknown seed protein (USP) from Vicia faba (Bassüner et al 1988), BNM2 from Brassica napus (Boutilier et al 1994;Treacy et al 1997), RD22, Sali3-2 from G. max (Ragland and Soliman 1997), and PG1β (β-subunit of polygalacturonase I) from Lycopersicon esculentum (Zheng et al 1992). Their expression patterns have some variety in terms of tissue specificity and the conditions for induction.…”