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PMID:21722378
| Citation |
Viollet, S, Fuchs, RT, Munafo, DB, Zhuang, F and Robb, GB (2011) T4 RNA ligase 2 truncated active site mutants: improved tools for RNA analysis. BMC Biotechnol. 11:72 |
|---|---|
| Abstract |
T4 RNA ligases 1 and 2 are useful tools for RNA analysis. Their use upstream of RNA analyses such as high-throughput RNA sequencing and microarrays has recently increased their importance. The truncated form of T4 RNA ligase 2, comprising amino acids 1-249 (T4 Rnl2tr), is an attractive tool for attachment of adapters or labels to RNA 3'-ends. Compared to T4 RNA ligase 1, T4 Rnl2tr has a decreased ability to ligate 5'-PO4 ends in single-stranded RNA ligations, and compared to the full-length T4 Rnl2, the T4 Rnl2tr has an increased activity for joining 5'-adenylated adapters to RNA 3'-ends. The combination of these properties allows adapter attachment to RNA 3'-ends with reduced circularization and concatemerization of substrate RNA. |
| Links |
PubMed PMC3149579 Online version:10.1186/1472-6750-11-72 |
| Keywords |
Adenosine Monophosphate/chemistry; Adenosine Monophosphate/metabolism; Analysis of Variance; Catalytic Domain; Electrophoresis, Polyacrylamide Gel; High-Throughput Screening Assays/methods; Hydrogen-Ion Concentration; Mutation; Polyethylene Glycols/chemistry; RNA/analysis; RNA/genetics; RNA/metabolism; RNA Ligase (ATP)/chemistry; RNA Ligase (ATP)/genetics; RNA Ligase (ATP)/isolation & purification; RNA Ligase (ATP)/metabolism; Viral Proteins/chemistry; Viral Proteins/genetics; Viral Proteins/isolation & purification; Viral Proteins/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0003909: DNA ligase activity |
ECO:0000314: |
F |
Figure 2 shows the ligation products of 3'-blocked and 5'- adenylated DNA and T4 RNA ligase 1/T4 RNL1 from Enterobacteria phage T4. |
complete | ||||
| GO:0003909: DNA ligase activity |
ECO:0000315: |
F |
Figure 7 compares the ligation products of T4 RNA ligase 2/T4 RNL2 and mutants of this protein in Enterobacteria phage T4. |
complete | ||||
Notes
See also
References
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