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Characterization of anther-expressed genes encoding a major class of extracellular oleosin-like proteins in the pollen coat of Brassicaceae.
Plant J. 1996 May; 9(5):625-37.PJ

Abstract

A large, heterogeneous, highly expressed gene family encoding oleosin-like proteins is described in the Brassicaceae. Seven related cDNA sequences were isolated from Brassica napus anther mRNA using RACE-PCR and compared with other recently described anther-specific oleosin-like genes from B. napus. The expression patterns of four representative members of this diverse gene family were analyzed by Northern blotting and in situ hybridization. In all cases, the genes were expressed specifically in the tapetum of 3-5 mm B. napus buds, which contained microspores at the late-vacuolate and bicellular stages of development. The predicted protein products are ordered into subclasses, each of which has a characteristic C-terminal domain, containing different amino acid motifs or repeated residues. Tryphine (pollen coat) fractions from mature B. napus pollen were found to be particularly enriched in polypeptides of apparent molecular weights 32-38 kDa, plus numerous less abundant polypeptides of less than 15 kDa. The N-terminal 15-20 residues of three of these polypeptides (12, 32 and 38 kDa) were found by microsequencing to be identical to parts of the predicted amino acid sequences of three of the tapetal-expressed oleosin-like genes. This indicates the possibility of post-translational modification of these proteins resulting in a cleavage of the primary translation products in order to generate the mature tryphine polypeptides. These data imply that a large and diverse group of oleosin-like proteins is synthesized in the tapetum of B. napus anthers and that following tapetal degradation, these proteins, possibly in modified form, then relocate to the developing microspores where they eventually constitute some of the major components of the extracellular tryphine of mature pollen grains. These proteins share a conserved 70 amino acid residue hydrophobic domain and are related structurally to the seed-specific intracellular oleosins, although their biological function may be different.

Authors+Show Affiliations

Department of Brassica and Oilseeds Research, John Innes Centre, Norwich, UK.No affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8653113

Citation

Ross, J H., and D J. Murphy. "Characterization of Anther-expressed Genes Encoding a Major Class of Extracellular Oleosin-like Proteins in the Pollen Coat of Brassicaceae." The Plant Journal : for Cell and Molecular Biology, vol. 9, no. 5, 1996, pp. 625-37.
Ross JH, Murphy DJ. Characterization of anther-expressed genes encoding a major class of extracellular oleosin-like proteins in the pollen coat of Brassicaceae. Plant J. 1996;9(5):625-37.
Ross, J. H., & Murphy, D. J. (1996). Characterization of anther-expressed genes encoding a major class of extracellular oleosin-like proteins in the pollen coat of Brassicaceae. The Plant Journal : for Cell and Molecular Biology, 9(5), 625-37.
Ross JH, Murphy DJ. Characterization of Anther-expressed Genes Encoding a Major Class of Extracellular Oleosin-like Proteins in the Pollen Coat of Brassicaceae. Plant J. 1996;9(5):625-37. PubMed PMID: 8653113.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of anther-expressed genes encoding a major class of extracellular oleosin-like proteins in the pollen coat of Brassicaceae. AU - Ross,J H, AU - Murphy,D J, PY - 1996/5/1/pubmed PY - 1996/5/1/medline PY - 1996/5/1/entrez SP - 625 EP - 37 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 9 IS - 5 N2 - A large, heterogeneous, highly expressed gene family encoding oleosin-like proteins is described in the Brassicaceae. Seven related cDNA sequences were isolated from Brassica napus anther mRNA using RACE-PCR and compared with other recently described anther-specific oleosin-like genes from B. napus. The expression patterns of four representative members of this diverse gene family were analyzed by Northern blotting and in situ hybridization. In all cases, the genes were expressed specifically in the tapetum of 3-5 mm B. napus buds, which contained microspores at the late-vacuolate and bicellular stages of development. The predicted protein products are ordered into subclasses, each of which has a characteristic C-terminal domain, containing different amino acid motifs or repeated residues. Tryphine (pollen coat) fractions from mature B. napus pollen were found to be particularly enriched in polypeptides of apparent molecular weights 32-38 kDa, plus numerous less abundant polypeptides of less than 15 kDa. The N-terminal 15-20 residues of three of these polypeptides (12, 32 and 38 kDa) were found by microsequencing to be identical to parts of the predicted amino acid sequences of three of the tapetal-expressed oleosin-like genes. This indicates the possibility of post-translational modification of these proteins resulting in a cleavage of the primary translation products in order to generate the mature tryphine polypeptides. These data imply that a large and diverse group of oleosin-like proteins is synthesized in the tapetum of B. napus anthers and that following tapetal degradation, these proteins, possibly in modified form, then relocate to the developing microspores where they eventually constitute some of the major components of the extracellular tryphine of mature pollen grains. These proteins share a conserved 70 amino acid residue hydrophobic domain and are related structurally to the seed-specific intracellular oleosins, although their biological function may be different. SN - 0960-7412 UR - https://www.unboundmedicine.com/medline/citation/8653113/Characterization_of_anther_expressed_genes_encoding_a_major_class_of_extracellular_oleosin_like_proteins_in_the_pollen_coat_of_Brassicaceae_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0960-7412&date=1996&volume=9&issue=5&spage=625 DB - PRIME DP - Unbound Medicine ER -