Comparative Genomics of Glycine max, Medicago truncatula, Other Legumes, and Arabidopsis thaliana

Author(s):  
Nevin Dale Young
Genome ◽  
2004 ◽  
Vol 47 (1) ◽  
pp. 141-155 ◽  
Author(s):  
H H Yan ◽  
J Mudge ◽  
D-J Kim ◽  
R C Shoemaker ◽  
D R Cook ◽  
...  

To gain insight into genomic relationships between soybean (Glycine max) and Medicago truncatula, eight groups of bacterial artificial chromosome (BAC) contigs, together spanning 2.60 million base pairs (Mb) in G. max and 1.56 Mb in M. truncatula, were compared through high-resolution physical mapping combined with sequence and hybridization analysis of low-copy BAC ends. Cross-hybridization among G. max and M. truncatula contigs uncovered microsynteny in six of the contig groups and extensive microsynteny in three. Between G. max homoeologous (within genome duplicate) contigs, 85% of coding and 75% of noncoding sequences were conserved at the level of cross-hybridization. By contrast, only 29% of sequences were conserved between G. max and M. truncatula, and some kilobase-scale rearrangements were also observed. Detailed restriction maps were constructed for 11 contigs from the three highly microsyntenic groups, and these maps suggested that sequence order was highly conserved between G. max duplicates and generally conserved between G. max and M. truncatula. One instance of homoeologous BAC contigs in M. truncatula was also observed and examined in detail. A sequence similarity search against the Arabidopsis thaliana genome sequence identified up to three microsyntenic regions in A. thaliana for each of two of the legume BAC contig groups. Together, these results confirm previous predictions of one recent genome-wide duplication in G. max and suggest that M. truncatula also experienced ancient large-scale genome duplications.Key words: Glycine max, Medicago truncatula, Arabidopsis thaliana, conserved microsynteny, genome duplication.


2003 ◽  
Vol 106 (7) ◽  
pp. 1256-1265 ◽  
Author(s):  
H. H. Yan ◽  
J. Mudge ◽  
D.-J. Kim ◽  
D. Larsen ◽  
R. C. Shoemaker ◽  
...  

2008 ◽  
Vol 9 (3) ◽  
pp. R57 ◽  
Author(s):  
Lei Li ◽  
Hang He ◽  
Juan Zhang ◽  
Xiangfeng Wang ◽  
Sulan Bai ◽  
...  

2021 ◽  
Vol 12 ◽  
Author(s):  
Xiaomin Ji ◽  
Xiaoyue Wu ◽  
Wei Chen ◽  
Qianhui Yuan ◽  
Yixin Shen ◽  
...  

Phosphoethanolamine methyltransferase (PEAMT), a kind of S-adenosylmethionine-dependent methyltransferases, plays an essential role in many biological processes of plants, such as cell metabolism, stress response, and signal transduction. It is the key rate-limiting enzyme that catalyzes the three-step methylation of ethanolamine-phosphate (P-EA) to phosphocholine (P-Cho). To understand the unique function of PEAMT in soybean (Glycine max) lipid synthesis, we cloned two phosphoethanolamine methyltransferase genes GmPEAMT1 and GmPEAMT2, and performed functional identification. Both GmPEAMT1 and GmPEAMT2 contain two methyltransferase domains. GmPEAMT1 has the closest relationship with MtPEAMT2, and GmPEAMT2 has the closest relationship with CcPEAMT. GmPEAMT1 and GmPEAMT2 are located in the nucleus and endoplasmic reticulum. There are many light response elements and plant hormone response elements in the promoters of GmPEAMT1 and GmPEAMT2, indicating that they may be involved in plant stress response. The yeast cho2 opi3 mutant, co-expressing Arabidopsis thaliana phospholipid methyltransferase (PLMT) and GmPEAMT1 or GmPEAMT2, can restore normal growth, indicating that GmPEAMTs can catalyze the methylation of phosphoethanolamine to phosphate monomethylethanolamine. The heterologous expression of GmPEAMT1 and GmPEAMT2 can partially restore the short root phenotype of the Arabidopsis thaliana peamt1 mutant, suggesting GmPEAMTs have similar but different functions to AtPEAMT1.


2021 ◽  
Vol 1 (19) ◽  
pp. 205-206
Author(s):  
I.V. Pinskiy

The characteristics of various miRNA binding sites in the mRNAs of the MYB transcription factor genes of Arabidopsis thaliana, Glycine max and Vitis vinifera have been established. The most conserved miRNA binding sites were the binding sites of the miR828 family.


2020 ◽  
Vol 27 (10) ◽  
pp. 1544-1552
Author(s):  
Pan Zou ◽  
Lijin Duan ◽  
Shasha Zhang ◽  
Xue Bai ◽  
Zhenghui Liu ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document