Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0268318 (
ICP
)
10,007
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
RNA is known to interact with Mg
2+
when assuming higher-ordered tertiary configurations. Structurally, when
tRNA
molecules interact with Mg
2+
, they consistently form a "L-shape" conformation each time they are synthesized. Therefore, if Mg
2+
can induce tertiary structure formation, then binding to alternative cations could produce alternative tertiary configurations. By utilizing circular dichroism and mobility gel-shift assays it was observed that
tRNA
structure can be altered when in the presence of different divalent cationic species. Formation of these alternative structural configurations was further validated by aminoacylating these
tRNA
structural anomalies with their native enzyme, which resulted in markedly different degrees of activity. Thus, it was confirmed that structural changes do occur when
tRNA
forms complexes with different cations. To better understand these structural changes, quantitative cation binding to
tRNA
was determined through titrations as well as
ICP
-OES analysis, which indicated that the metal ions can bind to the
tRNA
structure in specific and non-specific ways. Lastly, it was observed through stopped-flow kinetics that
tRNA
can associate/dissociate from different cations to varying degrees, thus forming cation-specific complexes at unique rates.
...
PMID:Characterization of tRNA
Leu
binding interactions with Cu
2+
and Pb
2+
and their biological implications. 2837 39
