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CEBP, a nuclear-encoded chloroplast protein, has been previously cloned as a putative transcription factor involved in ethylene signaling in carnation development and senescence. In order to more clearly define CEBP role and function, we carried out experiments to define its pattern of mRNA abundance and possible subcellular localization. Changes in CEBP mRNA abundance showed a dramatic drop from anthesis to open flower stage of development immediately preceding the ethylene climacteric associated with flower senescence. A similar but less dramatic decrease in CEBP was observed upon ethylene exposure, again before endogenous climacteric ethylene was observed. The pattern of CEBP mRNA abundance suggests a response to or involvement in the initial steps of the petal senescence process. GFP co-localization showed that a GFP–CEBP construct was directed to the nucleus, whereas a CEBP–GFP construct localized to the chloroplast. Nuclear localization was expected as CEBP was cloned as an ethylene-responsive element-binding protein or transcription factor. The role and function of CEBP in the chloroplast, however, remains unclear. Future lines of inquiry based on our results are discussed.
Hee,Young,Yoo,Mihaela,Iordachescu,Jun,Huang,EliseHennebert,Sang,sik,Kim,Sangchul,Rho,MathiasFoo,PatrickFlammang,HongboZeng,DaeheeHwang,J.,Herbert,Waite,Dong,Soo,Hwang 한국당과학회 2017 한국당과학회 학술대회 Vol.2017 No.01
The byssal threads of the fan shell Atrina pectinata are non-living functional materials intimately associated with living tissue, which provide an intriguing paradigm of bionic interface for robust load-bearing device. An interfacial load-bearing protein (A. pectinata foot protein-1, apfp-1) with L-3,4-dihydroxyphenylalanine (DOPA)-containing and mannose binding domains has been characterized from Atrina's foot. apfp-1 was localized at the interface between stiff byssus and the soft tissue by immunochemical staining and confocal Raman imaging, implying that apfp-1 is an interfacial linker between the byssus and soft tissue, that is, the DOPA-containing domain interacts with itself and other byssal proteins via Fe3+–DOPA complexes, and the mannose-binding domain interacts with the soft tissue and cell membranes. Both DOPA- and sugar-mediated bindings are reversible and robust under wet conditions. This work shows the combination of DOPA and sugar chemistry at asymmetric interfaces is unprecedented and highly relevant to bionic interface design for tissue engineering and bionic devices.