¶óÆæÆ®¦¢Ä«Æä¦¢ºí·Î±×¦¢´õº¸±â
¾ÆÄ«µ¥¹Ì Ȩ ¸í»çƯ°­ ´ëÇבּ¸½Ç޹æ Á¶°æ½Ç¹« µ¿¿µ»ó°­ÀÇ Çѱ¹ÀÇ ÀüÅëÁ¤¿ø ÇÐȸº° ³í¹®
ÇÐȸº° ³í¹®

Çѱ¹°Ç¼³°ü¸®ÇÐȸ
Çѱ¹°ÇÃà½Ã°øÇÐȸ
Çѱ¹µµ·ÎÇÐȸ
Çѱ¹»ý¹°È¯°æÁ¶ÀýÇÐȸ
Çѱ¹»ýÅÂÇÐȸ
Çѱ¹¼öÀÚ¿øÇÐȸ
Çѱ¹½Ä¹°ÇÐȸ
Çѱ¹½Ç³»µðÀÚÀÎÇÐȸ
Çѱ¹ÀÚ¿ø½Ä¹°ÇÐȸ
Çѱ¹ÀܵðÇÐȸ
Çѱ¹Á¶°æÇÐȸ
Çѱ¹Áö¹Ý°øÇÐȸ
Çѱ¹ÇÏõȣ¼öÇÐȸ
Çѱ¹È¯°æ»ý¹°ÇÐȸ
Çѱ¹È¯°æ»ýÅÂÇÐȸ

Çѱ¹½Ä¹°ÇÐȸ / v.44, no.1, 2001³â, pp.1-6

( Molecular Cloning and Characterization of a Rice PP2C, OsPP2C4 )
;;;; ;;;;
 
ÃÊ ·Ï
Protein phosphorylation and dephosphorylation are major regulatory mechanisms that cells use to transmit signals from their extracellular environment to the interior, Up to now, two structurally distinct groups of ser/thr phosphatases ave known of: the PP1/PP2A family and the PP2C family, Here, we focus our efforts to reveal the functions of the PP2C family in rice. It has been known that PP2C has diverse functions related to developments and stress responses. We have obtained a rice EST clone, OsPP2C4, that contained the highly conserved PP2C motifs. RNA gel-blot analysis showed that OsPPSC4 was expressed highly in panicles, while it was expressed weakly in seedling leaves, seedling roots, and mature leaves. Assay of the PP2C enzyme activity with a substrate, para-nitrophenyl phosphate, showed that OsPPSC4 encoded an active PP2C. Transgenic plants expressing the antisense construct of this clone were generated to study the functional roles of the PP2C clone in rice.
 
Ű¿öµå
dephosphorylation;phosphatase;phosphorlation;PP2C;rice;
 
Journal of Plant Biology / v.44, no.1, 2001³â, pp.1-6
Çѱ¹½Ä¹°ÇÐȸ
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200111921138590)
¾ð¾î : ¿µ¾î
³í¹® Á¦°ø : KISTI Çѱ¹°úÇбâ¼úÁ¤º¸¿¬±¸¿ø
¸ñ·Ïº¸±â
ȸ»ç¼Ò°³ ±¤°í¾È³» ÀÌ¿ë¾à°ü °³ÀÎÁ¤º¸Ãë±Þ¹æÄ§ Ã¥ÀÓÀÇ ÇѰè¿Í ¹ýÀû°íÁö À̸ÞÀÏÁÖ¼Ò ¹«´Ü¼öÁý °ÅºÎ °í°´¼¾ÅÍ
   

ÇÏÀ§¹è³ÊÀ̵¿