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1.
Plant Biol (Stuttg) ; 18(4): 577-84, 2016 Jul.
Article in English | MEDLINE | ID: mdl-26833779

ABSTRACT

Lilium longiflorum (Easter lily) vegetative propagation occurs through production of underground bulbs containing apical and axillary meristems. In addition, sexual reproduction is achieved by flowering of elongated shoots above the bulb. It is generally accepted that L. longiflorum has an obligatory requirement for vernalisation and that long day (LD) regime hastens flowering. However, the effect of bulb size and origin, with respect to axillary or apical meristems on flowering, as well as the interactions between these meristems are largely unknown. The aim of this study was to explore the effect of bulb size, vernalisation and photoperiod on L. longiflorum flowering. To this end, we applied vernalisation and photoperiod treatments to the different bulb sizes and used a system of constant ambient temperature of 25 °C, above vernalisation spectrum, to avoid cold-dependent floral induction during plant growth. Vernalisation and LD hasten flowering in all bulbs. Large, non-vernalised bulbs invariably remained at a vegetative stage. However, small non-vernalised bulbs flowered under LD conditions. These results demonstrate for the first time that cold exposure is not an obligatory prerequisite for L. longiflorum flowering, and that an alternative flowering pathway can bypass vernalisation in small bulbs. We suggest that apical dominance interactions determine the distinct flowering pathways of the apical and axillary meristems. Similar floral induction is achieved in propagated bulblets from scaling. These innovative findings in the field of geophyte floral induction represent valuable applicative knowledge for lily production.


Subject(s)
Lilium/physiology , Cold Temperature , Flowers/growth & development , Flowers/physiology , Flowers/radiation effects , Lilium/growth & development , Lilium/radiation effects , Meristem/growth & development , Meristem/physiology , Meristem/radiation effects , Photoperiod , Plant Roots/growth & development , Plant Roots/physiology , Plant Roots/radiation effects
2.
Zygote ; 4(2): 159-66, 1996 May.
Article in English | MEDLINE | ID: mdl-8913030

ABSTRACT

Adducin is a cytoskeletal protein that can function in vitro to bundle F-actin and to control the assembly of the F-actin/spectrin cytoskeletal network. The Drosophila Adducin-like (Add) locus (also referred to as hu-li tai shao (hts)) encodes a family of proteins of which several are homologous to mammalian adducin (Ding et al., Proc. Natl. Acad. Sci. USA 90, 2512-16, 1993; Yue & Spradling, Genes Dev. 6, 2443-54, 1992). We report the identification of two novel adducin isoforms: a 95 x 10(3) Mr form (ADD-95) and an 87 x 10(3) Mr form (ADD-87). We present a detailed analysis of the distribution patterns of ADD-95 and ADD-87 during oogenesis and embryogenesis. The isoforms are co-expressed in several cell- and tissue-types; however, only ADD-87 is present in mid- to late-stage oocytes. ADD-87 is present throughout the oocyte cortex at stages 9 and 10 of oogenesis but is detectable only at the anterior pole from stage 11 onward, correlated with localisation of Add-hts mRNA first to the cortex and then to the anterior pole of the oocyte. ADD-87 co-localises with F-actin and spectrin in the cortex of the oocyte through stage 10 of oogenesis, consistent with a possible role in cytoskeletal assembly or function predicted by mammalian studies.


Subject(s)
Calmodulin-Binding Proteins/metabolism , Drosophila/embryology , Embryo, Nonmammalian/metabolism , Oocytes/metabolism , Actins/metabolism , Animals , Blotting, Western , Calmodulin-Binding Proteins/genetics , Calmodulin-Binding Proteins/immunology , Female , Nervous System/embryology , Nervous System/metabolism , Oocytes/cytology , Oocytes/growth & development , Oogenesis , Ovarian Follicle/metabolism , Ovarian Follicle/physiology , Spectrin/metabolism
3.
Dev Genet ; 19(3): 249-57, 1996.
Article in English | MEDLINE | ID: mdl-8952067

ABSTRACT

Adducin is a cytoskeletal protein that can function in vitro to bundle F-actin and to control the assembly of the F-actin/spectrin cytoskeletal network. We previously reported cloning of the Drosophila Adducin-like (Add) locus [Ding et al., 1993] also referred to as hu-li tai shao (hts) [Yue and Spradling, 1992], and identification of two adducin-related protein isoforms: a 95 x 10(3) Mr form (ADD-95) and an 87 x 10(3) Mr form (ADD-87) [Zaccai and Lipshitz, 1996]. ADD-87 protein is present throughout the oocyte cortex at stages 9 and 10 of oogenesis but is restricted to its anterior pole from stage 11 onward. This ADD-87 protein localization is preceded by localization of Add-hts mRNA first to the cortex and then to the anterior pole of the oocyte. Mutation of the swallow gene results in delocalization of Add-hts mRNA and ADD-87 protein from the cortex of stage 9 and 10 oocytes, and from the anterior pole of later stage oocytes. Early embryos produced by swallow or Add-hts mutant females have severe defects in the distribution of F-actin and spectrin as well as abnormalities in nuclear division, nuclear migration, and cellularization. In addition to their cytoskeletal defects, embryos produced by swallow females have an abnormal anterior pattern because bicoid mRNA is delocalized from the anterior pole. In contrast, bicoid mRNA is still found at the anterior of embryos produced by Add-hts mothers. Thus swallow functions to restrict bicoid mRNA and Add-hts mRNA to the cortex of the oocyte. Cortical restriction of Add-hts mRNA and protein is required for the normal structure and function of the early embryonic F-actin/spectrin cytoskeleton. A defective embryonic cytoskeleton can be induced in either of two ways: (1) by delocalization of functional ADD from the oocyte cortex (as in swallow mutants), or (2) by reduction of ADD function while retaining its normal cortical localization during oogenesis (as in Add-hts mutants).


Subject(s)
Calmodulin-Binding Proteins/genetics , Cytoskeletal Proteins/genetics , Drosophila Proteins , Drosophila/metabolism , Homeodomain Proteins , RNA, Messenger/metabolism , Trans-Activators , Actins/metabolism , Animals , Cytoskeletal Proteins/metabolism , Drosophila/embryology , Drosophila/genetics , Female , Insect Hormones/genetics , Insect Hormones/metabolism , Male , Mutation , Oogenesis , RNA-Binding Proteins/genetics , RNA-Binding Proteins/metabolism , Spectrin/metabolism
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