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밀의 저분자 글루테닌 서브유닛 단백질

Low-molecular-weight Glutenin Subunits in Common Wheat (Triticum aestivum L.)

Jong-Yeol Lee1, Hye-Rang Beom1, Yeong-Tae Kim2, Sun-Hyung Lim1, Ung-Han Yoon1, Chang-Kug Kim1, Young-Joo Seol1, Chang-Hoon Lee1, Hye-Jung Lee1, Young-Mi Kim1,*
Korean Journal of Breeding Science 2014;46(4):342-352.
Published online: October 31, 2014

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*Corresponding Author : (ymikim@korea.kr, Tel: +82-63 - 238-4601, Fax: +82-63-238-4604)
• Received: October 15, 2014   • Revised: November 5, 2014   • Accepted: November 6, 2014

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  • Low-molecular-weight glutenin subunits (LMW-GS) play a crucial role in the processing quality of wheat flour. They are encoded multi gene family located at the Glu-A3, Glu-B3 and Glu-D3 on the short arm of chromosome 1A, 1B and 1D respectively. Typical LMW-GSs are composed of three parts including a short N-terminal domain, a relatively short repetitive domain and a C-terminal domain. Further, typical LMW-GS sequences are divided into LMW-s, LMW-m and LMW-i types, on the basis of the first amino acid of the mature proteins (serine, methionine and isoleucine, respectively). Although it is known that the allelic variation of LMW-GSs affect the properties of dough, it is still not clear which LMW-GSs confer better bread-making quality because of the larger number of expressed subunits and their overlapping mobility with abundant gliadin proteins. Therefore, it is important to characterize LMW-GS genes and develop functional markers to identify different LMW-GS alleles for application in wheat breeding. In this review, we discuss the various aspects of LMW-GS, including their structural characteristics, the development of marker, relationship between LMW-GSs and bread wheat quality, and genetic engineering of the LMW-GSs.
밀은 대략 BC 7500-6500년 전부터 경작된 인류 최초의 작 물이다. BC 6000-5000년 사이에 육배체 밀(T. aestivum) 과 엠머 밀(emmer wheat, T. timopheevi var. araraticum와 T. turgidum var. dicocoides)이 메소포타미아와 서이란 지역에 서 관개농업을 통해 경작되었다는 기록이 있다(Feldman 1995). 밀은 귀리나 보리와 같이 밀족(Triticeae)에 속하고 벼과 (Poaceae family)에서 가장 크고 중요한 속 중의 하나이다(Dewey 1984). 밀족은 일반적으로 Aegilops, Elymus, Hordeum, Secale, Triticum 5개의 속으로 구성된다(Löve 1984, Stebbins 1956). 밀속과 밀족에서 일반적으로 염색체수는 x = 7이다. 야생 이배체 밀 Triticum monococcum (AA 염색체), T. tauschii (DD 염색체) 와 T. speltoides (SS) 에서는 2n = 2x = 14개, 사배체 밀 T. turgidum (AABB 염색체)와 T. timopheevii (AAGG 염색체)는 2n = 4x = 28개이다(Feldman 1976). 보통밀 T. aestivum (AABBDD 염색체)은 6배체 밀로서, 2n = 6x = 42개의 염색 체를 가진다(Zohary & Hopf 1993).
밀 저장 단백질이 빵 만들기에 가장 중요한 역할을 한다고 알려져 있으며(Morrison 1988, Wall 1979), 빵 가공성은 정 성적으로 특정 단백질의 유무 및 특정 단백질 서브유닛의 유 무가 밀접한 관련성이 있다고 알려져 있다(Gupta et al. 1989, Johansson et al. 1998 and 2001, Payne et al. 1987). 밀가루 가 빵, 국수, 과자와 같은 다양한 가공적성을 가지는 것은 전 적으로 글루텐 단백질들에 기인한다(Weegels et al. 1996). 260여 년 전 Beccari에 의해 밀 글루텐 단백질 추출이 보고된 이후, 밀 글루텐 단백질의 추출방법에 따른 글루텐 단백질의 분류 와 글루텐 구조가 반죽에 미치는 기능적 특성을 밝히는 연구가 꾸준히 이어져오고 있다(Payne 1987, Shewry et al. 2002, Wieser 2007). 글루텐 단백질은 알콜 수용액 [60-70% (v/v) ethanol또는 50% (v/v) propan-1-ol]의 용해도에 따라 녹는 글리아딘과 녹지 않은 글루테닌으로 나눠진다(Wieser 2007). 글리아딘은 시스테인 잔기가 없어 이황화 결합이 없거 나, 있어도 분자 내 이황화 결합(intra-disulfide bond)를 형성 하며 단량체 형태로 존재한다.
밀 저장 단백질은 글루테닌과 글리아딘의 두개의 주된 단 백질로 구성되어 있다. 글루테닌은 고분자 글루테닌 서브유닛 [high-molecular-weight glutenin subunit (HMW-GS)]과 저 분자글루테닌 서브유닛 [low-molecular-weight glutenin subunit (LMW-GS)]으로 구성되며, HMW-GS는 1A, 1B, 1D 염색체 장완에 있는 Glu-A1, Glu-B1, Glu-D1에 의해 암호화되고 (Payne et al. 1980), LMW-GS는 1A, 1B, 1D 염색체 단완 에 있는 Glu-A3, Glu-B3 그리고 Glu-D3에 의해 암호화된다 (Gupta & Shepherd 1990, Jackson et al. 1996). 밀 품종에서 HMW-GS와 LMW-GS의 유전적 변이가 밀 반죽의 물성의 변화 및 가공성에 영향을 미친다고 보고되고 있다(D’Ovidio & Masci 2004, Nagamine et al. 2000).
국민 1인당 밀 소비량이 연간 32.4 kg으로 쌀 다음으로 높 지만, 최근 이상기후와 바이오 연료용 곡물 수요의 증가로 인한 국제 곡물 가격 상승으로 자급률이 2% 이하인 국내 현실에서 밀 자급률 향상은 어느 때 보다 절실한 실정이다(농업통계연 감 2011). 국내산 밀의 자급률 향상을 위해 숙기 단축과 수량성 및 재해 저항성 증진에 대한 연구가 활발히 진행되는 한편으 로, 밀의 가공적성에 많은 영향을 미치는 글루테닌의 기능 연구 를 위하여 국내 밀품종에 대한 SDS-PAGE나 STS (sequence tagged sites) 분자표지를 이용한 판별이 이루어지고 있다(Park et al. 2011).
본 총설에서는 글루텐 복합체(Gluten complex) 중에서도 가공적성에 많은 영향을 미치고 있지만 분석상의 어려움 때 문에 연구가 미진한 저분자글루테닌 서브유닛의(LMW-GS)의 분자 구조, 기능(quality property), 육종 현장에서 활용도가 높은 분자표지 마커 및 형질전환에 관해 기술하고자 한다.
밀 종자 저장 단백질의 1/3 정도를 차지하는 저분자 글루테닌 서브유닛(LMW-GS)은 글루텐의 신장성에 주로 관여하며, 고 분자 글루테닌(HMW-GS)과 결합을 통해 탄성에도 관여하는 것으로 알려져 있다(Bietz & Wall 1973, Cornish et al. 2001, Gianibelli et al. 2001). 이런 이유로 LMW-GS 의 발현 분석 통한 밀 품종 및 유전자원에 대한 평가와 LMW-GS 조성이 가 공적성에 미치는 영향에 대한 평가가 이루어지고 있다(Branlard et al. 2001 and 2003, Flaete & Uhlen 2003, Shan et al. 2007, Park et al. 2011).
LMW-GS를 조절하는 유전자는 1번 염색체 단완(short-arm) 에 위치해 있으며, 이들 유전자좌는 각각 Glu-A3, Glu-B3및 Glu-D3으로 명명되었다(Singh & Shepherd 1988). 이러한 Glu-3유전자는 γ및 ω글리아딘 발현에 관여하는 Gli-1 유전 자좌와 관련이 되어 있는 것으로 알려져 있다(Jackson et al. 1996). SDS-PAGE분석을 통한 LMW-GS 발현은, Glu-A3 유전자좌에서 6개의 패턴으로 알려져있고, Glu-B3 유전자좌 에서는 9개의 패턴이, Glu-D3 유전자좌에서 5개의 패턴으로 발현되어 전체적으로 20개의 LMW-GS 단백질이 발현되는 것으로 알려져 있다(Gupta & Shepherd 1990). 글루테닌 단 백질은 이차원전기영동 즉, 분자량과 등전점(isoelectric point, pI)에 따라 A, B, C 세 그룹으로 나뉘는데 A 그룹은 HMWGS, B 그룹은 전형적인 LMW-GS, C 그룹은 LMW-GS와 α/ β, γ 글리아딘의 혼합 그룹으로 존재한다(Fig. 1). 분자간 이 황화결합을 형성하는 시스테인 잔기의 위치 및 N-말단과 C- 말단의 아미노산의 배열에 따라 12 그룹으로 분류하기도 한 다(Ikeda et al. 2002, Juhász & Gianibelli 2003). 또한, LMW-GS는 성숙 단백질(mature protein)의 N-말단의 첫 아 미노산 잔기에 따라 LMW-i (이소루신), LMW-m (메치오닌) 그리고 LMW-s (세린)의 세 종류로 나뉜다(Cloutier et al. 2001, Lew et al. 1992). 이들 세 종류의 LMW-GS 단백질은 이차원 전기영동과 N-말단아미노산 서열분석에 의해 확인되었 다(Ikeda et al 2006, Lew et al. 1992, Maruyama-Funatsuki et al. 2004, Masci et al. 1998).
Fig. 1.
Two-dimensional gel electrophoresis (IEF × SDS-PAGE) of glutenin fraction of wheat cultivar Chinese Spring. The HMW-GS, LMW-GS and gliadin fractions are indicated.
KJBS-46-342_F1.gif
전형적인 LMW-GS의 구조는 Fig. 2와 3, Table 2에 나타 낸 바와 같이 20개 아미노산의 signal peptide, N-말단 부분, 비교적 짧은 서열의 반복 도메인 그리고 C-말단으로 구성되 어 있으며 i-타입 LMW-GS의 경우 N-말단 부분이 다른 타입 의 LMW-GS들과 달리 바로 ISQQQQ-의 서열로 시작한다. LMW-s 타입은 모든 밀 품종들에서 가장 발현량이 많으며 평균 분자량(35,000-45,000 daltons)도 LMW-m타입(30,000- 40,000 daltons)보다 크다(Lew et al. 1992, Masci et al. 1998, Tao & Kasarda 1989). LMW-s 타입의 N-말단 아미노산 서 열은 현재까지 SHIPGL- 하나만 보고된 반면, LMW-m 타입은 METSHIPGL-, MENSHIPGL-, METSHIPSL-, METSRVPGL-, METSRIPGL-, 그리고 METSCIPGL-로 다양하다(Ikeda et al. 2002 and 2006, Kasarda 1989, Lew et al. 1992, Masci et al. 1998, Tao & Kasarda 1989). Table 2에 Glu-A3, Glu-B3 및 Glu-D3 유래의 LMW-GS 단백질의N-말단 서열에 관하여 정리하였다. Ikeda et al. (2006)은 LMW-s타입의 SHIPGL- 서열은 LMW-m 타입의 METSHIPGPL- 서열이 asparaginyl peptidase에 의해 전사후변형(post-translational modification) 으로 인해N-말단의 3개 잔기가 절단되었다고 제시하고 있다. 이와 유사한 현상이 오메가 글리아딘에서도 보고되었다(DuPont et al. 2004).
Fig. 2.
Diagrams representing the structures of typical LMW-GSs as deduced amino acids from their genes. The grey and black stars indicate cysteins involved in inter-molecular and intra-molecular bonds, respectively. Sig; signal peptide, N-ter; N-terminal domain; Rep; repetitive domain and C-ter; C-terminal domain.
KJBS-46-342_F2.gif
Fig. 3.
Alignments of deduced amino acid sequences of Glu-A3, Glu-B3 and Glu-D3allelic variants. Identical residues are shaded. The position of cystein residues are marked with filled down arrow. Sig; signal peptide, N-ter; N terminal domain; Rep; repetitive domain and C-ter; C-terminal domain and these positions are marked with filled nabla. GluD3-1 specific hydrophobic residues are underlined. GluA3-1 specific glutamine repeats are also underlined.
KJBS-46-342_F3.gif
Table 2.
N-terminal amino acid sequences of the deduced Glu-A3, Glu-B3 and Glu-D3 proteins.
Table 2.
Locus Genes N-terminal amino acid sequence Type based on the first amino acid Type (Group) based on Ikeda et al. Reference
Glu-A3 GluA3-1 ISQQQQ(Q/P/A)P- LMW-i VI (11 &12) Wang et al. 2010
GluA3-2 GluA3-2 LMW-m IV(6)
GluA3-3z ISQQQQQ- LMW-i
Glu-B3 GluB3-1 MENSHIPGL- LMW-m II(3) Wang et al. 2009
GluB3-2 MENSHIPGL- LMW-m II(3)
GluB3-3 MENSHIPGL- LMW-m II(3)
GluB3-4 METSHIPSL- LMW-m I (2)
Glu-D3 GluD3-1 METSRVPGL- LMW-m III (5) Zhao et al. 2007
GluD3-2 METRCIPGL- LMW-m V (10)
GluD3-3 (M/IEN)SHIPGL- LMW-s II (4)
GluD3-4 METSCISGL- LMW-m IV (7)
GluD3-5 METSHIPGL- LMW-m I (1)
GluD3-6 METSCIPGL- LMW-m IV (8 & 9)

z GluA3-3 have four allelic variants and they are all pseudo genes

LMW-GS는 분자 내 그리고 분자 간 이황화결합을 형성하 는 8개의 시스테인을 포함하며 분자 간 이황화결합을 형성하 는 시스테인의 위치에 따라 2개로 분류된다(Fig. 2, Fig. 3). LMW-m, LMW-s 타입은 N-말단 부분 또는 반복 도메인 위 치에 시스테인 잔기가 1개, C-말단에 나머지 1개가 존재하며 LMW-i 타입은 C-말단에 분자 간 이황화결합을 형성하는 2 개의 시스테인 잔기가 존재한다. 또한 Fig. 3의 밑줄 부분에 나타낸 바와 같이 i-타입 LMW-GS (GluA3-1)의 경우 C- 말 단 I 부분에 6개의 글루타민의 반복이 보이며, METSRVPGL- 로 시작하는 GluA3-1는 반복도메인에 PVIILQQ와 같은 소 수성 잔기들이 존재하였다. 이와 같이 반복 도메인에 반복 모 티프의 삽입 또는 결실 그리고 분자간 이황화 결합을 형성하 는 시스테인 잔기의 위치 차이가 기능의 차이와 관련이 되어 있을 것으로 추론하고 있다(Ikeda et al. 2002, Wieser 2007).
6배체 밀의 HMW-GS의 경우 3~5개의 서브유닛이 있고 SDS-PAGE에 의해 확인이 가능하기 때문에 이를 이용한 기 능 연구가 잘 확립되어 있다(Shewry et al. 1992 and 2003). LMW-GS의 경우 총 종자 저장 단백질의 1/3, 글루테닌 단백 질 중에서 60%를 차지하고, 밀가루 가공성에 많은 영향을 미 침에도 불구 하고 SDS-PAGE 조사에서 단백질 밴드 패턴을 파악하기 힘들고 LMW-GS와 글리아딘이 상당 부분 중복되 기 때문에 개별 LMW-GS와 유전자 좌 변이에 따른 기능연구 가 HMW-GS에 비해 어려움이 많다(Gupta et al. 1994, Maruyama- Funatsuki et al. 2004, Masci et al. 1998). 따라 서 LMW-GS 유전자 좌를 구별 할 수 있는 마커 개발이 필요하 였다(Andesrsen & Lubberstedt 2003, Zhang et al. 2004).
현재 일반적으로 Glu-A3, Glu-B3 그리고 Glu-D3 유전자 좌에 대한 STS 마커가 개발되어 있지만, 육종 현장에서는 Glu-A3 (Wang et al. 2010), Glu-B3 (Wang et al. 2009) 마 커만 사용하고 있다(http://maswheat.ucdavis.edu/protocols/ FunctionalMarkers/FM_quality.htm#wang2009b). Table 1에 나타낸 것처럼 Glu-D3 유전자 좌 마커는 특정Glu-D3 유전자 만을 구분하기 때문에 아직 범용으로는 사용되지 못하고 있다. 유전자 좌특이 마커는 지금까지 Glu-A3 위치에는 7개(a, b, c, d, e, f, g), Glu-B3 위치에는 9개(a, b, c, d, e f, g, h, i) 그리고 Glu-D3 위치에는 5개(a, b, c, d, e, f ) 등 21개의 유 전자 좌(SDS-PAGE mobility에 의한 분류)에 대해 확인하여 육종 현장에 많이 사용하고 있다(Gupta & Shepherd 1990, Jackson et al. 1996, Zhang et al 2004). 또한 새로운 LMWGS 유전자 좌를 발견하고 마커화 하려는 시도가 보고되고 있 다(McIntosh et al. 2008). Wang et al. (2010)은 밀 품종 Aroona (GluA3c)와 6개의 Aroona 근동질 계통(gluA3a, b, d, e, f)과 밀 품종Glenlea (GluA3g)를 이용하여 Glu-A3 위치 에서 유전자 특이 프라이머로 GluA3-1, GluA3-2, 그리고 GluA3-3의 전장 open reading frame (ORF)를 나타내는 유 전자들을 분리하였고, SDS-PAGE 분류법에 의한 gluA3a, gluA3b, gluA3ac (Glu-A3a와 c를 구별), gluA3d, gluA3e, gluA3f, gluA3g 유전자 좌 구별이 가능한 프라이머를 제작하 였으며, 또한 Glu-A3b + Glu-A3f, Glu-A3d + Glu-A3f, Glu-A3d + Glu-A3f 그리고 Glu-A3b + Glu-A3e를 구별할 수 있는 다중 검출 마커(multiplex marker)를 개발하여 141 개 CIMMYT 밀 품종에서 검증하였다. Glu-B3 위치에서는 8 개의 Aroona (Glu-B3b)와Aroona 근동질 계통(Glu-B3a, c, d, f, g, h, i)과 밀 품종Cheyenne (Glu-B3e)를 이용하여 유전 자 특이 프라이머로 GluB3-1, GluB3-2, GluB3-3 그리고 GluB3-4 완전한 ORF를 지닌 유전자들을 분리하였고, 위의 9개 유전자 좌 구분을 위한 gluB3a, gluB3b, gluB3c, gluB3d, gluB3e, gluB3fg (Glu-B3f와 g를 구별), gluB3g, gluB3h, gluB3i, gluB3bef (Glu-B3b, e, f를 구별)유전자 좌 특이 프라 이머를 제작하였고 161개의 품종 및 후대라인에서 검증하였 다(Wang et al. 2009). Glu-D3 위치에서는 Chinese Spring (Glu-D3a), BT2288A (Glu-D3e), Silverstar (Glu-D3b), Sunco (Glu-D3b), Aroona (Glu-D3c), Norin 61 (Glu-D3d), Tasman (Glu-D3a), Hartog (Glu-D3e)의 8개의 보통 밀 품 종을 이용하여 유전자 특이 프라이머로 GluD3-11, GluD3-12, GluD3-21, GluD3-22, GluD3-23, GluD3-31, GluD3-32, GluD3-41, GluD3-42, GluD3-43, GluD3-5, GluD3-6의 12 종류의 유전자를 분리하였고, 이중 GluD3-5와 GluD3-6는 모든 품종에서 이들 유전자를 공통으로 가지고 있는 것을 확 인하였다. 또한 GluD3-21/22, GluD3-22, GluD3-23, GluD3-31, GluD3-32, GluD3-41, GluD3-43에 특이적인 STS를 개발하 여 Glu-D3a, b, c 그리고 f를 가지는 중국 밀 20개 품종에서 검증하였다(Zhao et al. 2006 and 2007). Table 1에서는 Glu-3 각각의 유전자 좌를 구별하기 위한 STS 마커 프라이 머를 표시하였고, Fig. 3에서 Glu-A3, Glu-B3 그리고 Glu-D3 유전자들의 유추 아미노산을 나타내었다.
Table 1.
Allele-specific PCR markers for the discrimination of Glu-3 alleles defined by protein mobility in common wheat.
Table 1.
Locus Marker/ Target gene Sequence (5’-3’) Allele Expected fragment size (bp) Chromosome Reference
Glu-A3 gluA3a LA1F: AAACAGAATTATTAAAGCCGG SA1R: GGTTGTTGTTGTTGCAGCA Glu-A3a 529 1AS Wang et al. 2010
gluA3b LA3F: TTCAGATGCAGCCAAACAA SA2R:GCTGTGCTTGGATGATACTCTA Glu-A3b 894
gluA3d LA3F: TTCAGATGCAGCCAAACAA SA4R: TGGGGTTGGGAGACACATA Glu-A3d 967
gluA3e LA1F: AAACAGAATTATTAAAGCCGG SA5R: GGCACAGACGAGGAAGGTT Glu-A3e 158
gluA3f LA1F: AAACAGAATTATTAAAGCCGG SA6R: GCTGCTGCTGCTGTGTAAA Glu-A3f 552
gluA3g LA1F: AAACAGAATTATTAAAGCCGG SA7R:AAACAACGGTGATCCAACTAA Glu-A3g 1345
gluA3ac LA1F: AAACAGAATTATTAAAGCCGG SA3R: GTGGCTGTTGTGAAAACGA Glu-A3a Glu-A3c 573
Glu-B3 gluB3a SB1F: CACAAGCATCAAAACCAAGA SB1R: TGGCACACTAGTGGTGGTC Glu-B3a 1095 1BS Wang et al. 2009
gluB3b SB2F: ATCAGGTGTAAAAGTGATAG SB2R: TGCTACATCGACATATCCA Glu-B3b 1570
gluB3c SB3F: CAAATGTTGCAGCAGAGA SB3R: CATATCCATCGACTAAACAAA Glu-B3c 472
gluB3d SB4F: CACCATGAAGACCTTCCTCA SB4R: GTTGTTGCAGTAGAACTGGA Glu-B3d 662
gluB3e SB5F: GACCTTCCTCATCTTCGCA SB5R: GCAAGACTTTGTGGCATT Glu-B3e 669
gluB3g SB7F: CCAAGAAATACTAGTTAACACTAGTC SB7R: GTTGGGGTTGGGAAACA Glu-B3g 853
gluB3h SB8F: CCACCACAACAAACATTAA SB8R: GTGGTGGTTCTATACAACGA Glu-B3h 1022
gluB3i SB9F: TATAGCTAGTGCAACCTACCAT SB9R: TGGTTGTTGCGGTATAATTT Glu-B3i 621
gluB3bef SB10F: CATCAACAACAAATAGTACTAGAA SB10R: GGCGGGTCACACATGACA Glu-B3b Glu-B3e 750
gluB3fg SB6F: TATAGCTAGTGCAACCTACCAT SB6R: CAACTACTCTGCCACAACG Glu-B3f Glu-B3g 812
Glu-D3 GluD3-21/22 M2F12: TTGGGCCTAATCGCTCGC M2R12: TAGTCTCCATCTGCGCAATT Glu-D3b Glu-D3a 884 1DS Zhao et al. 2007
GluD3-22 M2F2: CTCGTCTTTGCCCTCCTCA M2R2: CTAAACAACGGTGACCCAAT Glu-D3b? Glu-D3a? 958
GluD3-23 M2F3: TCTGTACTTTGTGTGTGATCG M2R3: ACTGCTGCTGGAGGAATAG Glu-D3f Glu-D3c 725
GluD3-31 M3F1:ACAAGTGCCATTGCACAAATG M3R1: GATAGATGGATGAACAAATA Glu-D3a Glu-D3b 528
GluD3-32 M3F2: CAAGTGCCATTGCACAAATT M3R2: AATGATGGTTGTTGCGGTAT Glu-D3f Glu-D3c 334
GluD3-41 M4F1: AAGTAGTTAGCACCAATCCAT M4R1: CCTGTTGTTGTTGTTGTTGTT Ndz 773
GluD3-43 M4F3:GCATCAAAACCAAGCAAAAG M4R3: GGCTGAACAATAGGGATTTA Ndz 413

znd: not detected

LMW-GS 단백질이 HMW-GS 보다 많이 발현되고 함량 도 많지만, 가공적성에 미치는 영향에 대해서는 연구가 미흡 하고, 발현되는 각 단백질에 대한 연구도 밝혀진 것이 거의 없는 실정이다. 그 원인으로 SDS-PAGE에 의해 분리되는 LMW-GS 양상이 글리아딘과 유사한 양상을 보여 분자량에 따른 동정이 어렵기 때문이다(Appelbee et al. 2009, D’Ovidio & Masci 2004). 이차원 전기영동(2DE) 분석 방법은 1차원 SDS-PAGE 보다 훨씬 많은 정보를 제공하므로 LMW-GS 발현 단백질의 정성 및 정량 분석으로 보다 정밀하고 다양한 자료를 제시할 수 있으며, 최근에는 2차원 전기영동과 MALDITOF- MS (matrix-assisted laser desorption / ionization time-of-flight mass spectrometry)와 같은 펩타이드 질량분 석법의 결합을 통한 LMW-GS 분석이 실시되고 있다(Liu et al. 2010). 또한, 최근 글루테닌 관련 유전자서열 특이적 분자 표지를 활용한 분석이 많이 이루어지고 있으며 (Gale 2005), 육종의 효율성을 높이고자 Glu-1및 Glu-3의 다중검출 PCR 마커를 활용하는 연구가 수행되고 있다 (Liang et al. 2010, Salmaowicz & Moczulski 2004, Sui et al. 2010, Wang et al. 2010, Zhang et al. 2008).
HMW-GS와 제빵적성과의 관계는 폭넓게 연구되었다. 예 를 들어 HMW-GS 5 + 10 단백질이 HMW-GS 2 + 12에 비 해 좋은 제빵적성을 가진다고 보고되었다(Payne et al. 1980 and 1987). 하지만 LMW-GS의 제빵적성에 관련한 연구는 아직 시작단계에 불과하다. 최근의 연구들에서 LMW-GS도 HMW-GS 만큼 제빵적성에 중요한 역할을 한다는 결과들이 보고되고 있는데, 초강력분인 Canadian Western Extra-Strong (CWES)의 특정 LMW-GS를 일본 밀 품종에 도입한 근동질 계통에서 밀반죽의 물성이 강화되었다(Takata et al. 2001). 또한 CWES와 일본 밀 품종의 재조합 계통들에서 KS2로 명 명된 42kDa의 LMW-GS가 비슷한 크기의 LMW-GS인 HS1 에 비해 제빵 적성에서 더 좋은 결과를 보였고, HMW-GS 5 + 10과 KS2, HMW-GS 5 + 10과 HS1 그리고 HMW-GS 2 + 12과 KS2, HMW-GS 2 + 12과 KS2의 조합 실험에서도 HMW-GS 5 + 10과 KS2라인에서 가장 좋은 결과를 보였는 데, 이는 특정 LMW-GS 단백질이 밀반죽 물성에 많은 영향을 미 친다는 것을 보여주고 있다(Maruyama-Funatuski et al. 2004).
일반적으로 LMW 글루테닌 구성성분들이(allelic composition) 이 보통밀에서 반죽강도(dough strength) 및 신장성 (extensibility)에 영향을 미친다고 알려져 있으며, 이것은 LMW-GS와 HMW-GS가 중합체를 형성하고, 이 중합체가 단량체인 글리아딘과의 결합하여 글루텐 복합체(Gluten complex) 를 형성하고 밀반죽 물성(dough rheological property)에 영 향을 미친다고 보고되었다(Gupta et al. 1989 and 1994, Nieto-Taladriz et al. 1994, Payne et al. 1987, Ruiz & Carrillo 1995, Sontag-Strohm et al. 1996). Glu-3 위치에서 특정 LMW-GS 유전자 좌가 반죽강도 그리고 신장성에 영향을 미 치는 것이 밝혀졌는데, 여러 문헌에서 Glu-A3, Glu-B3 및 Glu-D3 유전자 좌와 밀반죽 품질(dough quality effects)의 관계를 정립하였다(Gupta et al. 1989, 1990, 1991 and 1994, Metakovsky et al. 1990). Rmax (maximum dough resistance) 값은 Glu-A3 유전자 좌에서 b>d>e>c, Glu-B3 유전자 좌에 서 i>b=a>e=f=g=h>c 그리고 Glu-D3에서 e>b>a>c>d의 순 서를 보였다. 신장성 부분에서는 Glu-B3 bbb (각각 Glu-A3, Glu-B3 및 Glu-D3)의 조합일 때 최고의 값을 보이고, bbc 또 한 좋은 결과 값을 보였다(Cornish et al. 1993).
중국과 호주 공동연구 그룹에서 특정 LMW-GS 유전자 좌 (allele)의 기능 연구를 위해 호주 밀 품종인 Aroona에 5개의 Glu-A3 (b, c, d, e, f) 라인, 9개의 Glu-B3 (a, b, c, d, e, f, g, h, i)라인 그리고 5개의 Glu-D3 (a, b, c, d, f) 근동질 계통 을 이용하여 밀반죽의 품질인자(quality parameter)를 측정하 였는데 이 중 Glu-A3d, Glu-B3b, Glu-B3g, Glu-B3i 라인들 에서 좋은 제빵 품질을 보였고, Glu-D3 유전자 좌들에서는 미미한 결과를 보였다(Zhang et al. 2012). 이러한 결과들을 볼 때 국내에서 우수한 제빵 적성을 가진 밀 품종 육성을 위 해서는 상기의 LMW-GS 유전자 좌의 도입이 시급할 것으로 생각된다.
LMW-GS단백질의 구조, 유전자 좌 분석, 유전자 발현과 밀가루 반죽의 물성과의 관계에서 탄성에 관여하는 메카니즘 등을 연구하는 주된 이유는 밀의 가공적성을 개량하는데 있 다. 지금까지의 연구는 특정 밀 품종에서 글루테닌과 글리아 딘의 정성적인 분석과 기능과의 관계를 연구하는데 집중되어 있었다면 앞으로는 분석 기술의 발달과 함께 밀 반죽 물성에 많은 영향을 미치는 정량적인 요인 즉, 글루테닌 단백질의 절 대량(glutenin quantity), 글리아딘 단백질의 절대량(gliadin quantity), 글리아딘 단백질과 글루테닌 단백질의 구성비 (gliadin / glutenin ratio), 고분자 글루테닌 단백질과 저분자 글루테닌 단백질의 구성비(HMW-GS / LMW-GS ratio)와 같은 요소들과 기능과의 관계를 분석하는 연구에 집중하여야 할 것이다(Veraverbeke et al. 2002).
LMW-GS가 밀 글루텐 복합체 에서 많은 역할을 하고 밀 가루 가공적성의 중요한 결정인자 임에도 이들의 분자구조와 기능에 관한 연구는 아직 미미하다. 이러한 이유로 밀의 가공 적성 개량 및 밀가루 반죽에서의 기능 연구를 위해 안정적이 고 재현성 있는 밀 형질전환 기술을(Vasil et al. 1992, Weeks et al. 1993)을 이용하여 여분의 LMW-GS 유전자를 추가적 으로 도입하는 시도가 진행되어 왔다. Masci et al. (2003)은 밀 품종 Cheyenne에서 Glu-D3 유래의 5’ 및3’ 인접서열 (flanking sequence)을 포함하는 1,200 bp와 1,600 bp 두 유 전자를 분리하여 보통 밀인 Bob White에 유전자 총(Biolistic transformation)을 이용하여 과발현 형질전환체를 육성하였 고, Southern blot과 2DE로 유전자 삽입과 도입 LMW-GS 단백질 발현을 확인하였다. 기능분석을 위해 형질전환체 밀가 루와 비형질전환체의 밀가루에서 SDS 침강법 실험을 한 결 과 비형질전환체의 밀가루가 형질전환체 보다 높은 값을 보 였는데 이것은 글루텐 단백질의 양 보다 특정 LMW-GS가 기능에 영향을 미친다는 것을 나타내고 있다. Araki et al. (2008)은 HMW-GS 1By9와 i 타입 LMW-GS (이케다 분류 법에 의한 그룹 11)을 벼 글루테린 돌연변이체인 LGC1에 아 그로박테리움법으로 형질 전환하였고 1차원 및 2차원 전기영 동으로 HMW-GS와 LMW-GS 단백질 발현을 확인하였다. 또한 각각의 형질전환체를 교배하여 HMW-GS와 LMW-GS 모두 벼 저장 단백질 중합체에 분자간 이황화결합에 의해 삽 입되었음을 보여주었다.
현재 일반적으로 LMW-GS 유전자는 Glu-A3 위치에서 GluA3-1, GluA3-2, GluA3-3의 3종류 Glu-B3 위치에서는 GluB3-1, GluB3-2, GluB3-3, GluB3-4 등 4종류 그리고 Glu-B3 위치에서는 GluD3-1, GluD3-2, GluD3-3, GluD3-4, GluD3-5, GluD3-6의 6종류의 유전자가 존재하며, 각각의 위 치(loci)에서 아미노산의 삽입, 결실, 변이에 의해 차이를 보 이게 되며, 각 Glu-A3, Glu-B3 및 Glu-D3 유전자 좌는 2~3 개의 유전자와 Pseudo gene으로 구성된다(Wang et al. 2009, Wang et al. 2010, Zhao et al. 2006 and 2007). 이들 각 유 전자들의 구조에 따른 기능적 차이를 보기 위해서는 이들 각 종류의 유전자별로 과발현 형질전환체를 제작하여 밀 반죽 물성을 확인해보거나, 대장균이나 효모, 곤충을 이용하여 발 현시킨 재조합 단백질(Gali 1989, Tamas & Shewry 2006)을 base flour에 혼합하여 물성의 변화를 분석하는 등의 협력연 구를 통해 분자적 수준에서의 LMW-GS 단백질의 기작과 기 능 분석 연구가 이루어져야 한다. 이러한 연구를 통해 축적된 자료를 기반으로 하여 강력분 및 가공적성 맞춤형 밀 품종 육 종이나 형질전환체 육성이 이루어져야 소비자 맞춤형 밀 생 산 및 다양성이 있는 식량 자원 확보에 기여를 할 것이다.
밀가루에서 저분자 글루테닌 서브유닛(LMW-GS)의 유전 적 변이가 고분자 글루테닌 서브유닛(HMW-GS) 만큼 밀 반 죽의 물성의 변화 및 가공적성에 많은 영향을 미친다. 총 글 루테닌 단백질의60 % 정도를 차지하는 LMW-GS는 밀반죽 의 신장성에 주로 관여하며, HMW-GS와 분자간 이황화 결 합을 통해 중합체를 형성하여 탄성에 영향을 미치며, 또한 단 량체인 글리아딘과 글루텐 중합체를 형성하여 밀반죽 특유의 물성을 나타낸다. 하지만, LMW-GS가 많은 기능을 가졌음에 도 불구하고 다수의 유전자(multi-gene)으로 존재하고 글리아 딘과의 혼재성으로 인해 유전자 좌 분석과 개별 단백질의 기 능 연구에 어려움이 있지만, 많은 수의 LMW-GS유전자에 대 한 연구가 진행되어 유전자서열 특이적 분자표지를 활용한 분석이 많이 이루어지고 있다. LMW-GS의 기능 연구를 위해 근동질 계통이나 재조합 계통을 이용하여 특정 유전자 좌와 빵 가공성(bread-making quality)에 관한 분석이 이루어졌으 며, 특정 LMW-GS 유전자의 기능 분석을 위해 형질전환체 분석이나 재조합발현을 통한 분석에 의한 연구가 진행되고 있다. 또한 정성적인 기능 분석과 더불어 글리아딘 단백질과 글루테닌 단백질의 비율 또는 HMW-GS와 LMW-GS의 비율 과 같은 정량적인 분석 결과와 기능과의 상관관계를 해명하 는 연구도 진행되어야 할 것이다.
본 연구는 농촌진흥청 국립농업과학원 농업과학기술 연구 개발사업(과제번호: PJ010116)의 지원에 의해 이루어진 것임.
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Low-molecular-weight Glutenin Subunits in Common Wheat (Triticum aestivum L.)
Korean. J. Breed. Sci.. 2014;46(4):342-352.   Published online December 31, 2014
DOI: https://doi.org/10.9787/KJBS.2014.46.4.342
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Low-molecular-weight Glutenin Subunits in Common Wheat (Triticum aestivum L.)
Korean. J. Breed. Sci.. 2014;46(4):342-352.   Published online December 31, 2014
DOI: https://doi.org/10.9787/KJBS.2014.46.4.342
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Low-molecular-weight Glutenin Subunits in Common Wheat (Triticum aestivum L.)
Image Image Image
Fig. 1. Two-dimensional gel electrophoresis (IEF × SDS-PAGE) of glutenin fraction of wheat cultivar Chinese Spring. The HMW-GS, LMW-GS and gliadin fractions are indicated.
Fig. 2. Diagrams representing the structures of typical LMW-GSs as deduced amino acids from their genes. The grey and black stars indicate cysteins involved in inter-molecular and intra-molecular bonds, respectively. Sig; signal peptide, N-ter; N-terminal domain; Rep; repetitive domain and C-ter; C-terminal domain.
Fig. 3. Alignments of deduced amino acid sequences of Glu-A3, Glu-B3 and Glu-D3allelic variants. Identical residues are shaded. The position of cystein residues are marked with filled down arrow. Sig; signal peptide, N-ter; N terminal domain; Rep; repetitive domain and C-ter; C-terminal domain and these positions are marked with filled nabla. GluD3-1 specific hydrophobic residues are underlined. GluA3-1 specific glutamine repeats are also underlined.

Fig. 1.

Fig. 2.

Fig. 3.

Low-molecular-weight Glutenin Subunits in Common Wheat (Triticum aestivum L.)

N-terminal amino acid sequences of the deduced Glu-A3, Glu-B3 and Glu-D3 proteins.

Locus Genes N-terminal amino acid sequence Type based on the first amino acid Type (Group) based on Ikeda et al. Reference
Glu-A3 GluA3-1 ISQQQQ(Q/P/A)P- LMW-i VI (11 &12) Wang et al. 2010
GluA3-2 GluA3-2 LMW-m IV(6)
GluA3-3z ISQQQQQ- LMW-i
Glu-B3 GluB3-1 MENSHIPGL- LMW-m II(3) Wang et al. 2009
GluB3-2 MENSHIPGL- LMW-m II(3)
GluB3-3 MENSHIPGL- LMW-m II(3)
GluB3-4 METSHIPSL- LMW-m I (2)
Glu-D3 GluD3-1 METSRVPGL- LMW-m III (5) Zhao et al. 2007
GluD3-2 METRCIPGL- LMW-m V (10)
GluD3-3 (M/IEN)SHIPGL- LMW-s II (4)
GluD3-4 METSCISGL- LMW-m IV (7)
GluD3-5 METSHIPGL- LMW-m I (1)
GluD3-6 METSCIPGL- LMW-m IV (8 & 9)

z GluA3-3 have four allelic variants and they are all pseudo genes

Allele-specific PCR markers for the discrimination of Glu-3 alleles defined by protein mobility in common wheat.

Locus Marker/ Target gene Sequence (5’-3’) Allele Expected fragment size (bp) Chromosome Reference
Glu-A3 gluA3a LA1F: AAACAGAATTATTAAAGCCGG SA1R: GGTTGTTGTTGTTGCAGCA Glu-A3a 529 1AS Wang et al. 2010
gluA3b LA3F: TTCAGATGCAGCCAAACAA SA2R:GCTGTGCTTGGATGATACTCTA Glu-A3b 894
gluA3d LA3F: TTCAGATGCAGCCAAACAA SA4R: TGGGGTTGGGAGACACATA Glu-A3d 967
gluA3e LA1F: AAACAGAATTATTAAAGCCGG SA5R: GGCACAGACGAGGAAGGTT Glu-A3e 158
gluA3f LA1F: AAACAGAATTATTAAAGCCGG SA6R: GCTGCTGCTGCTGTGTAAA Glu-A3f 552
gluA3g LA1F: AAACAGAATTATTAAAGCCGG SA7R:AAACAACGGTGATCCAACTAA Glu-A3g 1345
gluA3ac LA1F: AAACAGAATTATTAAAGCCGG SA3R: GTGGCTGTTGTGAAAACGA Glu-A3a Glu-A3c 573
Glu-B3 gluB3a SB1F: CACAAGCATCAAAACCAAGA SB1R: TGGCACACTAGTGGTGGTC Glu-B3a 1095 1BS Wang et al. 2009
gluB3b SB2F: ATCAGGTGTAAAAGTGATAG SB2R: TGCTACATCGACATATCCA Glu-B3b 1570
gluB3c SB3F: CAAATGTTGCAGCAGAGA SB3R: CATATCCATCGACTAAACAAA Glu-B3c 472
gluB3d SB4F: CACCATGAAGACCTTCCTCA SB4R: GTTGTTGCAGTAGAACTGGA Glu-B3d 662
gluB3e SB5F: GACCTTCCTCATCTTCGCA SB5R: GCAAGACTTTGTGGCATT Glu-B3e 669
gluB3g SB7F: CCAAGAAATACTAGTTAACACTAGTC SB7R: GTTGGGGTTGGGAAACA Glu-B3g 853
gluB3h SB8F: CCACCACAACAAACATTAA SB8R: GTGGTGGTTCTATACAACGA Glu-B3h 1022
gluB3i SB9F: TATAGCTAGTGCAACCTACCAT SB9R: TGGTTGTTGCGGTATAATTT Glu-B3i 621
gluB3bef SB10F: CATCAACAACAAATAGTACTAGAA SB10R: GGCGGGTCACACATGACA Glu-B3b Glu-B3e 750
gluB3fg SB6F: TATAGCTAGTGCAACCTACCAT SB6R: CAACTACTCTGCCACAACG Glu-B3f Glu-B3g 812
Glu-D3 GluD3-21/22 M2F12: TTGGGCCTAATCGCTCGC M2R12: TAGTCTCCATCTGCGCAATT Glu-D3b Glu-D3a 884 1DS Zhao et al. 2007
GluD3-22 M2F2: CTCGTCTTTGCCCTCCTCA M2R2: CTAAACAACGGTGACCCAAT Glu-D3b? Glu-D3a? 958
GluD3-23 M2F3: TCTGTACTTTGTGTGTGATCG M2R3: ACTGCTGCTGGAGGAATAG Glu-D3f Glu-D3c 725
GluD3-31 M3F1:ACAAGTGCCATTGCACAAATG M3R1: GATAGATGGATGAACAAATA Glu-D3a Glu-D3b 528
GluD3-32 M3F2: CAAGTGCCATTGCACAAATT M3R2: AATGATGGTTGTTGCGGTAT Glu-D3f Glu-D3c 334
GluD3-41 M4F1: AAGTAGTTAGCACCAATCCAT M4R1: CCTGTTGTTGTTGTTGTTGTT Ndz 773
GluD3-43 M4F3:GCATCAAAACCAAGCAAAAG M4R3: GGCTGAACAATAGGGATTTA Ndz 413

znd: not detected

Table 2. N-terminal amino acid sequences of the deduced Glu-A3, Glu-B3 and Glu-D3 proteins.

GluA3-3 have four allelic variants and they are all pseudo genes

Table 1. Allele-specific PCR markers for the discrimination of Glu-3 alleles defined by protein mobility in common wheat.

nd: not detected

Table 2.

Table 1.

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