Differential regulation of phenylalanine ammonia lyase activity and protein level by light in tomato seedlings

dc.contributor.author Sreelakshmi, Yellamaraju
dc.contributor.author Sharma, Rameshwar
dc.date.accessioned 2022-03-27T03:48:42Z
dc.date.available 2022-03-27T03:48:42Z
dc.date.issued 2008-04-01
dc.description.abstract Red light, acting via phytochrome, stimulates phenylalanine ammonia lyase (PAL) activity in cotyledons and hypocotyls of tomato seedlings. The time course of photoinduction of PAL activity has a peak level at 4 h after which activity declines significantly. In tomato seedlings PAL activity comprised of three isoforms and light stimulated activity of all three isoforms. A polyclonal antibody raised against PAL purified from tomato leaves recognized PAL protein belonging to PAL-II and PAL-III isoforms. The mode of increase in PAL activity was investigated by immunochemical techniques. The photostimulated increase in PAL activity appeared to be dependent on de novo synthesis of protein and nucleic acid. However, inhibition of protein phosphatase activity blocked increase in PAL activity without affecting the increase in PAL protein levels. The results indicate that in addition to de novo synthesis, the photostimulation of PAL activity likely requires dephosphorylation by a type 2C protein phosphatase. © 2008 Elsevier Masson SAS. All rights reserved.
dc.identifier.citation Plant Physiology and Biochemistry. v.46(4)
dc.identifier.issn 09819428
dc.identifier.uri 10.1016/j.plaphy.2008.02.001
dc.identifier.uri https://www.sciencedirect.com/science/article/abs/pii/S0981942808000181
dc.identifier.uri https://dspace.uohyd.ac.in/handle/1/5589
dc.subject Phenylalanine ammonia lyase
dc.subject Phosphorylation
dc.subject Phytochrome
dc.subject Protein inactivation
dc.subject Tomato
dc.title Differential regulation of phenylalanine ammonia lyase activity and protein level by light in tomato seedlings
dc.type Journal. Article
dspace.entity.type
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