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Acid detergent lignin, lodging resistance index, and expression of the caffeic acid O-methyltransferase gene in brown midrib-12 sudangrass.

Li Y, Liu G, Li J, You Y, Zhao H, Liang H, Mao P - Breed. Sci. (2015)

Bottom Line: The research showed that the mean ADL content of bmr-12 mutants (20.94 g kg(-1)) was significantly (P < 0.05) lower than measured in N-12 lines (43.45 g kg(-1)), whereas the LRI of bmr-12 mutants (0.29) was significantly (P < 0.05) higher than in N-12 lines (0.22).There was no significant correlation between the two indexes in bmr-12 materials (r = -0.44, P > 0.05).The relative expression level of COMT gene was significantly reduced, which likely led to the decreased ADL content observed in the bmr-12 mutant.

View Article: PubMed Central - PubMed

Affiliation: Department of Grassland Science, College of Animal Science and Technology, China Agricultural University , Beijing 100193 , China ; Dryland Farming Institute, Hebei Academy of Agricultural and Forestry Sciences , Hengshui 053000 , China.

ABSTRACT
Understanding the relationship between acid detergent lignin (ADL) and lodging resistance index (LRI) is essential for breeding new varieties of brown midrib (bmr) sudangrass (Sorghum sudanense (Piper) Stapf.). In this study, bmr-12 near isogenic lines and their wild-types obtained by back cross breeding were used to compare relevant forage yield and quality traits, and to analyze expression of the caffeic acid O-methyltransferase (COMT) gene using quantitative real time-PCR. The research showed that the mean ADL content of bmr-12 mutants (20.94 g kg(-1)) was significantly (P < 0.05) lower than measured in N-12 lines (43.45 g kg(-1)), whereas the LRI of bmr-12 mutants (0.29) was significantly (P < 0.05) higher than in N-12 lines (0.22). There was no significant correlation between the two indexes in bmr-12 materials (r = -0.44, P > 0.05). Sequence comparison of the COMT gene revealed two point mutations present in bmr-12 but not in the wild-type, the second mutation changed amino acid 129 of the protein from Gln (CAG) to a stop codon (UAG). The relative expression level of COMT gene was significantly reduced, which likely led to the decreased ADL content observed in the bmr-12 mutant.

No MeSH data available.


Amino acid sequences of SsCOMT, SbCOMT, OsCOMT, TaCOMT, AtCOMT, and ZmCOMT were initially aligned by DNAMAN6.0 using default parameters, and followed by manual alignment. Sequences used: SsCOMT (KJ101565), SbCOMT (AEM63601), OsCOMT (ABF72191), TaCOMT (AAP23942), AtCOMT (AAB96879), and ZmCOMT (AAQ24337). Dark shading represents 100% conservation. The S-adenosyl-L-methionine (SAM) binding domain (LVDVGGGxG) was conserved in COMTs. Catalytic residues are marked by arrows, and active site substrate bind/positioning residues marked by asterisks. Numbers indicate the position from the start codon.
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f2-65_291: Amino acid sequences of SsCOMT, SbCOMT, OsCOMT, TaCOMT, AtCOMT, and ZmCOMT were initially aligned by DNAMAN6.0 using default parameters, and followed by manual alignment. Sequences used: SsCOMT (KJ101565), SbCOMT (AEM63601), OsCOMT (ABF72191), TaCOMT (AAP23942), AtCOMT (AAB96879), and ZmCOMT (AAQ24337). Dark shading represents 100% conservation. The S-adenosyl-L-methionine (SAM) binding domain (LVDVGGGxG) was conserved in COMTs. Catalytic residues are marked by arrows, and active site substrate bind/positioning residues marked by asterisks. Numbers indicate the position from the start codon.

Mentions: Sequence comparison with functionally characterized COMT proteins from various plants revealed high degrees of similarity, both at the nucleotide and amino acid level. The S-adenosyl-L-methionine (SAM) binding domain LVDVGGGxG, a signature of O-methyltransferases, was conserved in SsCOMT. Catalytic residues and active site substrate binding residues were also conserved in SsCOMT (Fig. 2). The conserved binding domains and residues were all located at expected positions in SsCOMT.


Acid detergent lignin, lodging resistance index, and expression of the caffeic acid O-methyltransferase gene in brown midrib-12 sudangrass.

Li Y, Liu G, Li J, You Y, Zhao H, Liang H, Mao P - Breed. Sci. (2015)

Amino acid sequences of SsCOMT, SbCOMT, OsCOMT, TaCOMT, AtCOMT, and ZmCOMT were initially aligned by DNAMAN6.0 using default parameters, and followed by manual alignment. Sequences used: SsCOMT (KJ101565), SbCOMT (AEM63601), OsCOMT (ABF72191), TaCOMT (AAP23942), AtCOMT (AAB96879), and ZmCOMT (AAQ24337). Dark shading represents 100% conservation. The S-adenosyl-L-methionine (SAM) binding domain (LVDVGGGxG) was conserved in COMTs. Catalytic residues are marked by arrows, and active site substrate bind/positioning residues marked by asterisks. Numbers indicate the position from the start codon.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4542929&req=5

f2-65_291: Amino acid sequences of SsCOMT, SbCOMT, OsCOMT, TaCOMT, AtCOMT, and ZmCOMT were initially aligned by DNAMAN6.0 using default parameters, and followed by manual alignment. Sequences used: SsCOMT (KJ101565), SbCOMT (AEM63601), OsCOMT (ABF72191), TaCOMT (AAP23942), AtCOMT (AAB96879), and ZmCOMT (AAQ24337). Dark shading represents 100% conservation. The S-adenosyl-L-methionine (SAM) binding domain (LVDVGGGxG) was conserved in COMTs. Catalytic residues are marked by arrows, and active site substrate bind/positioning residues marked by asterisks. Numbers indicate the position from the start codon.
Mentions: Sequence comparison with functionally characterized COMT proteins from various plants revealed high degrees of similarity, both at the nucleotide and amino acid level. The S-adenosyl-L-methionine (SAM) binding domain LVDVGGGxG, a signature of O-methyltransferases, was conserved in SsCOMT. Catalytic residues and active site substrate binding residues were also conserved in SsCOMT (Fig. 2). The conserved binding domains and residues were all located at expected positions in SsCOMT.

Bottom Line: The research showed that the mean ADL content of bmr-12 mutants (20.94 g kg(-1)) was significantly (P < 0.05) lower than measured in N-12 lines (43.45 g kg(-1)), whereas the LRI of bmr-12 mutants (0.29) was significantly (P < 0.05) higher than in N-12 lines (0.22).There was no significant correlation between the two indexes in bmr-12 materials (r = -0.44, P > 0.05).The relative expression level of COMT gene was significantly reduced, which likely led to the decreased ADL content observed in the bmr-12 mutant.

View Article: PubMed Central - PubMed

Affiliation: Department of Grassland Science, College of Animal Science and Technology, China Agricultural University , Beijing 100193 , China ; Dryland Farming Institute, Hebei Academy of Agricultural and Forestry Sciences , Hengshui 053000 , China.

ABSTRACT
Understanding the relationship between acid detergent lignin (ADL) and lodging resistance index (LRI) is essential for breeding new varieties of brown midrib (bmr) sudangrass (Sorghum sudanense (Piper) Stapf.). In this study, bmr-12 near isogenic lines and their wild-types obtained by back cross breeding were used to compare relevant forage yield and quality traits, and to analyze expression of the caffeic acid O-methyltransferase (COMT) gene using quantitative real time-PCR. The research showed that the mean ADL content of bmr-12 mutants (20.94 g kg(-1)) was significantly (P < 0.05) lower than measured in N-12 lines (43.45 g kg(-1)), whereas the LRI of bmr-12 mutants (0.29) was significantly (P < 0.05) higher than in N-12 lines (0.22). There was no significant correlation between the two indexes in bmr-12 materials (r = -0.44, P > 0.05). Sequence comparison of the COMT gene revealed two point mutations present in bmr-12 but not in the wild-type, the second mutation changed amino acid 129 of the protein from Gln (CAG) to a stop codon (UAG). The relative expression level of COMT gene was significantly reduced, which likely led to the decreased ADL content observed in the bmr-12 mutant.

No MeSH data available.