1992
DOI: 10.1016/0168-9452(92)90133-7
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A Brassica napus mRNA encoding a protein homologous to phospholipid transfer proteins, is expressed specifically in the tapetum and developing microspores

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Cited by 58 publications
(34 citation statements)
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“…This pattern of expression correlates well with the timing of lipid accumulation in the tapetum of the B. napus cv. Westar (Polowick and Sawhney, 1990) and with the expression of a phospholipid transfer protein found in the B. napus tapetum and microspores (Foster et al, 1992).…”
Section: Discussionmentioning
confidence: 99%
“…This pattern of expression correlates well with the timing of lipid accumulation in the tapetum of the B. napus cv. Westar (Polowick and Sawhney, 1990) and with the expression of a phospholipid transfer protein found in the B. napus tapetum and microspores (Foster et al, 1992).…”
Section: Discussionmentioning
confidence: 99%
“…The oleo-pollenin is considered the major protein component of the pollenkitt (Murphy & Ross, 1998;Murhpy, 2001). LTP genes are specifically expressed in the tapetum and developing microspores of Brassica napus, Nicotiana tabacum, Lilium henryi and Zea mays (Koltunow et al 1990;Foster et al, 1992;Crossley et al, 1995;Lauga et al, 2000). Therefore, the detection of nsLTPs in the A. latifolia pollenkitt is an expected result, because one of the many functions attributed to the pollenkitt is to protect the pollen protoplast from fungi and bacteria (Paccini & Hesse, 2005), and the localisation of nsLTPs in the pollenkitt confirms this hypothesis.…”
Section: The Role Of Nsltpsmentioning
confidence: 99%
“…It has been demonstrated that LTPs represent the most abundant protein associated with the extracellular wax of sporopollenin (68,69). Sporopollenin is built from extracellular lipids originating from the tapetum (56,70), and LTP function has been suggested to be involved in the transfer of these lipids to the microspore (71). The deposition of the exine begins soon after the completion of meiosis II (56) at the time the rice plants become most susceptible to cold damage.…”
Section: Identification Of Cold-responsive Proteins In Rice Anthersmentioning
confidence: 99%