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园艺学报 ›› 2014, Vol. 41 ›› Issue (5): 869-880.

• 蔬菜 • 上一篇    下一篇

甘蓝开花抑制因子FLC 家族氨基酸序列差异及其对FLC/SVP 聚合化的影响

刘智宇,杨朴丽*,江 为,谷慧英,王志敏,宋 明**,汤青林**   

  1. 西南大学园艺园林学院,南方山地园艺学教育部重点实验室,重庆市蔬菜学重点实验室,重庆 400715
  • 出版日期:2014-05-25 发布日期:2014-05-25

Differences of FLC Family Members and Its Effect on Dimerization of
FLC/SVP in Brassica oleracea

  1. College of Horticulture and Landscape Architecture,Southwest University;Key Laboratory of Horticulture Science for
    Southern Mountainous Regions,Ministry of Education;Key Laboratory of Olericulture,Chongqing 400715,China
  • Online:2014-05-25 Published:2014-05-25

摘要: 为深入研究甘蓝Flowering Locus C(FLC)家族与SHORT VEGETATIVE PHASE(SVP)蛋
白互作的分子机理及其对开花的调控作用,从甘蓝‘ZQ-67’材料中克隆了5 个FLC 家族基因(记为
BoFLCy1 ~ BoFLCy5)。它们均编码MIKC 型蛋白,按进化关系其编码蛋白可分为两类:BoFLCy3 和BoFLCy5
为第Ⅰ类,仅在C 域有1 个位点变异;BoFLCy1、BoFLCy2 和BoFLCy4 为第Ⅱ类,仅在K、C 域分别有1、
2 个位点变异。酵母双杂交显示:甘蓝BoFLC 家族蛋白均可与BoSVP 蛋白互作;但BoFLCy4 蛋白最为敏
感,其N 端插入3 个氨基酸TET 会破坏该作用。β–半乳糖苷酶活性分析表明:BoFLCy1 ~ BoFLCy5 与
BoSVP 互作强度差异显著,强弱关系为:BoFLCy1 > BoFLCy2 > BoFLCy3 > BoFLCy5 > BoFLCy4,该家族蛋
白KC 域内的变异位点若为疏水氨基酸则有利于FLC/SVP 聚合。进一步分析突变BoFLCy4 蛋白IK 域内
的保守位点发现:蛋白作用强度可能不受I 域的这些保守性亲(疏)水氨基酸(第63、77 位)影响,而
会受到K 域保守氨基酸(第120、121、135、157 位)的亲(疏)水性调节。

关键词: 甘蓝, 开花调节, FLC, SVP, 酵母双杂交, 作用强度

Abstract: The transcription factors Flowering Locus C(FLC)and SHORT VEGETATIVE PHASE
(SVP)interact to delay the flowering time in the plants of Brassica oleracea,but the molecular
mechanisms have not been thoroughly understood. In an effort to unravel the mechanisms of the protein
interactions,five FLC genes(named BoFLCy1–BoFLCy5) were cloned in Brassica oleracea. And all the
FLC family members encoded MIKC-type proteins which were classified into two groups. Group one has
two members(BoFLCy3 and BoFLCy5)with only one variational amino acid in C domain. While group two has three members(BoFLCy1,BoFLCy2 and BoFLCy4)with one or two variational amino acid positions in
K or C domain,respectively. Then yeast two-hybrid system was used in the experiments and showed that
all the BoFLCs(BoFLCy1–BoFLCy5)could act with BoSVP protein,but the three amino acids of TET
inserted into the N-terminal of BoFLCy4 may destroy the protein interaction. Furthermore , the
β-galactosidase activities were tested and indicated that the relationships of significantly different strengths
among BoFLCs/BoSVP were BoFLCy1 > BoFLCy2 > BoFLCy3 > BoFLCy5 > BoFLCy4. The hydrophobic
amino acids,which lied in the variational positions in KC domains of BoFLCs,were helpful for the
polymerization of FLCs/SVP. And the conservative amino acids,positions of 63,77,120,121,135 and
157 in IK domains of BoFLCy4,were respectively mutated and then acted with BoSVP protein. The results
suggested that these hydrophilic or hydrophobic amino acids in K domain not in I domain regulated and
affected the interaction strength.

Key words: Brassica oleracea, flowering regulation, FLC, SVP, yeast two-hybrid system, interaction strength

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