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Çѱ¹ÀÚ¿ø½Ä¹°ÇÐȸ / v.16, no.3, 2003³â, pp.257-263
´õ´ö¿¡¼­ Nucleoside Diphosphate Kinase 1 ºÐ¸® ¹× ºÐ¼®
( Isolation and Characterization of Nucleoside Diphosphate Kinase 1 of Codonopsis lanceolata )
±èÁ¾ÇÐ;¾ç´öÃá; ¢ß¹ÙÀÌ¿ÀÇǾÆ;°æÈñ´ëÇб³ »ý¸í°úÇдëÇÐ ¹× ÇѹæÀç·á°¡°ø¼¾Å¸;
 
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´õ´öÀÇ Àç¹è´Â ¼öÀͼºÀÌ ³ô°í Àç¹è¸éÀûµµ Áõ°¡ÇÏÁö¸¸ ¼ö¿ä¸¦ ¸¸Á·½Ãų ¸¸Å­ °ø±ÞÀÌ µû¸£Áö ¸øÇϰí ÀÖ´Ù. ¶ÇÇÑ Àç ¹è »óÀÇ ¾î·Á¿îÁ¡Àº º´ÃæÇØ, ±â°è¼öÈ®¿¡ ÀÇÇÑ ´ë±Ô¸ð Àç¹è¸¦ ´õ¿í´õ °ï¶õÇÏ°Ô Çϰí ÀÖ´Â ½ÇÁ¤ÀÌ´Ù. ÀÌ·¯ÇÑ ¹®Á¦Á¡ ¹× ȯ°æÀû ½ºÆ®·¹½º¿¡ ÀúÇ×ÇÏ¿© ÀÚ¶ö ¼ö ÀÖ´Â ½Ä¹°Ã¼¸¦ ¾ò±â À§ÇØ ´õ´öÀÇ cDNA¸¦ ºÐ¼®ÇÏ¿© ½ºÆ®·¹½º °üÇÑ À¯ÀüÀÚ Nucleoside diphosphates kinase 1(NDK 1)À» ºÐ¸®ÇÏ¿© ºÐ¼®ÇÏ¿© 148°³ÀÇ ¾Æ¹Ì³ë»ê ¼­¿­°ú ´Ù¸¥ ½Ä¹°Ã¼µéÀÇ NDK 1°ú ³ôÀº À¯»ç¼ºÀ» °¡Áø´Ù´Â °ÍÀ» ¾Ë¾Ò°í, ´õ´öÀÇ °¢ Á¶Á÷¿¡¼­ ³ªÅ¸³ª´Â ClNDK1ÀÇ ¹ßÇöÀ» ¾Ë¾Æº¸±â À§ÇØ Ä¶·¯½º, ÀÙ, ÁÙ±â, »Ñ¸® Á¶Á÷ÀÇ Àüü RNA¸¦ ÃßÃâÇÏ¿© cDNA¸¦ ÇÕ¼ºÇϰí PCRÀ» ¼öÇàÇÏ¿´´Ù RT¡©PCR ºÐ¼® °á°ú, ClNDK1Àº Á¶Á÷ ƯÀ̼º ¾øÀÌ Ä¶·¯½º, ÀÙ, ÁÙ±â, »Ñ¸® Á¶Á÷¿¡ ´ëÇØ¼­ ¸ðµÎ ¹ßÇöÀÌ µÇ¾úÀ¸¸ç, ¹ßÇö·®, ¿ª½Ã Å« Â÷ÀÌ ¾øÀÌ ¸ðµç Á¶Á÷¿¡¼­ µ¿ÀÏÇÏ°Ô ¹ßÇöµÇ¾ú´Ù. NDKs ´Â ȯ°æ ½ºÆ®·¹½º¿¡ ÀúÇ×¼ºÀ» °¡Áø´Ù°í ¾Ë·ÁÁ® ÀÖÁö¸¸ NDK 1 ´ëÇÑ ¿¬±¸´Â ¾ÆÁ÷±îÁö ºÎÁ·ÇÑ »óÅÂÀÌ´Ù. ¿ì¸®´Â ´õ´ö¿¡¼­ ºÐ¸®ÇÑ ClNDK1ÀÇ ½ºÆ®·¹½º ÀúÇ×¼º¿¡ ´ëÇØ¼­ Áö¼ÓÀûÀ¸·Î ¿¬±¸¸¦ ¼öÇà ÇÒ °ÍÀÌ´Ù.
The NDK1 is an ubiquitous enzyme that transfer phosphate groups from triphosphate nucleoside diphosphates(NDPs) in eukaryotes and prokaryotes. We isolated and characterized a cDNA encoding a nucleoside diphosphate kinase 1(CNDK 1) in Codonopsis lanceolata. The CNDK 1 is 444bp long and open reading frame of 447bp with a deduced amino acid of 148 residue. The CNDK 1 has an ATP binding site in 12¡©16 residue and phosphohistidine intermediate in 115 residue of amino acid sequence. Although several NDK 1 genes have been cloned in plants, but little is known about the functional significance of this enzyme during plant growth and development. The CNDK 1 shows the identities to Arabidopsis thaliana (71£¥), Oryza sativa(75£¥), Glycine max (79£¥), Brassica rapa (77£¥), Mesembryanthemum crystallinum (85 £¥), Spinacia oleracea (83£¥), Pisum sativum (82£¥). The CNDK 1 of C. laceolata have a closer relationship of Glycine max and Pisum sativum at the phylogenic analysis.
 
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ubiquitous enzyme;ATP binding site;phosphohistidine;
 
Çѱ¹ÀÚ¿ø½Ä¹°ÇÐȸÁö / v.16, no.3, 2003³â, pp.257-263
Çѱ¹ÀÚ¿ø½Ä¹°ÇÐȸ
ISSN : 1226-3591
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200311922145563)
¾ð¾î : Çѱ¹¾î
³í¹® Á¦°ø : KISTI Çѱ¹°úÇбâ¼úÁ¤º¸¿¬±¸¿ø
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