作物学报
作物學報
작물학보
ACTA AGRONOMICA SINICA
2014年
12期
2176-2182
,共7页
刘正帅%刘贵芬%杨明煜%贾晓%李运祥%赵法茂
劉正帥%劉貴芬%楊明煜%賈曉%李運祥%趙法茂
류정수%류귀분%양명욱%가효%리운상%조법무
小麦%淀粉分支酶%支链淀粉%时空表达%器官分布
小麥%澱粉分支酶%支鏈澱粉%時空錶達%器官分佈
소맥%정분분지매%지련정분%시공표체%기관분포
Triticum aestivum L.%Starch branching enzyme%Amylpectin%Spatiotemporal expression%Organ localization
为阐明小麦支链淀粉合成的酶学机制,以8个小麦品种的籽粒为材料,采用非变性聚丙烯酰胺凝胶电泳(Native-PAGE)和 SDS 聚丙烯酰胺凝胶电泳(SDS-PAGE)鉴定 SBE 同工酶类型、时空表达谱及亚基组成,分析 SBE 同工酶空间分布特点和器官表达特异性。共检测到4种 SBE 同工酶,其中 B 和 SBEIIa 分布在胚乳和叶片中,而 A 和Di 专一定位于胚乳中。在小麦籽粒灌浆过程中, Di 和 SBEIIa 首先表达,而后是 B, A 最后表达;至灌浆末期, B 和SBEIIa 停止表达。SBE 同工酶都是单亚基酶,均由一条86~92 kD 的多肽链组成。SBE 同工酶的空间分布具有器官特异性,并在籽粒发育进程中顺序表达。Di、B 和 SBEIIa 是占主导地位的 SBE 同工酶,可能是决定 SBE 总酶活性的主效应酶,在籽粒和叶片支链淀粉合成中起关键作用。
為闡明小麥支鏈澱粉閤成的酶學機製,以8箇小麥品種的籽粒為材料,採用非變性聚丙烯酰胺凝膠電泳(Native-PAGE)和 SDS 聚丙烯酰胺凝膠電泳(SDS-PAGE)鑒定 SBE 同工酶類型、時空錶達譜及亞基組成,分析 SBE 同工酶空間分佈特點和器官錶達特異性。共檢測到4種 SBE 同工酶,其中 B 和 SBEIIa 分佈在胚乳和葉片中,而 A 和Di 專一定位于胚乳中。在小麥籽粒灌漿過程中, Di 和 SBEIIa 首先錶達,而後是 B, A 最後錶達;至灌漿末期, B 和SBEIIa 停止錶達。SBE 同工酶都是單亞基酶,均由一條86~92 kD 的多肽鏈組成。SBE 同工酶的空間分佈具有器官特異性,併在籽粒髮育進程中順序錶達。Di、B 和 SBEIIa 是佔主導地位的 SBE 同工酶,可能是決定 SBE 總酶活性的主效應酶,在籽粒和葉片支鏈澱粉閤成中起關鍵作用。
위천명소맥지련정분합성적매학궤제,이8개소맥품충적자립위재료,채용비변성취병희선알응효전영(Native-PAGE)화 SDS 취병희선알응효전영(SDS-PAGE)감정 SBE 동공매류형、시공표체보급아기조성,분석 SBE 동공매공간분포특점화기관표체특이성。공검측도4충 SBE 동공매,기중 B 화 SBEIIa 분포재배유화협편중,이 A 화Di 전일정위우배유중。재소맥자립관장과정중, Di 화 SBEIIa 수선표체,이후시 B, A 최후표체;지관장말기, B 화SBEIIa 정지표체。SBE 동공매도시단아기매,균유일조86~92 kD 적다태련조성。SBE 동공매적공간분포구유기관특이성,병재자립발육진정중순서표체。Di、B 화 SBEIIa 시점주도지위적 SBE 동공매,가능시결정 SBE 총매활성적주효응매,재자립화협편지련정분합성중기관건작용。
This study aimed at disclosing the enzymatic mechanism in amylopectin synthesis in wheat (Triticum aestivum L.). The isozyme forms, organ localization, spatiotemporal expression profile and subunits constitution of starch branching enzyme (SBE) were identified in eight wheat cultivars from different provenances using native polyacrylamide gel electrophoresis (Native-PAGE) and SDS-PAGE. Four SBE isozymes were detected in wheat endosperm, in which isozymes B and SBEIIa were localized in en-dosperm and leaf, whereas isozymes A and Di were exclusively present in endosperm. In the process of grain filling, Di and SBEIIa expressed first, followed by isozyme B, and isozyme A expressed finally. However, B and SBEIIa terminated to express at late filling stage. All SBE isozymes were composed of one subunit of 86–92 kD, and their spatial localization exhibited organ specificity. According to the expression level, Di, B, and SBEIIa are considered as dominant isozymes for grain endosperm de-velopment. They probably determinate the total SBE activity and serve as key factors in amylpectin biosynthesis in wheat grain and leaf.