1997
DOI: 10.7124/bc.00048e
|View full text |Cite
|
Sign up to set email alerts
|

Studies of interaction sites between tRNA2Ser from Thermus thermophilus and seryl-tRNA synthetase by chemical modification

Abstract: Институт молекулярной биологии и генетики НАН Украины 252143, Киев, ул. Академика Заболотного, 150 Изучена реакционная способность остатков фосфорной кислоты тРНКг™ из Т. thermophilus, находящейся в комплексе с серил-тРНК синтетазой. Серил-тРНК синтетаза из Т. thermophilus защищает от модификации нитрозоэтилмочевиной фосфаты акцепторного, вариабельного и Т-стеблей, а также Т-петли.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

1
1
0

Year Published

2013
2013
2013
2013

Publication Types

Select...
1

Relationship

1
0

Authors

Journals

citations
Cited by 1 publication
(2 citation statements)
references
References 18 publications
1
1
0
Order By: Relevance
“…Furthermore, this recognition is based on the shape rather than on the specific nucleotide sequence, which fits well with the biochemical data [26,27]. These data are also in good agreement with those obtained by us in the solution, where SerRS TT protected from alkylation by ethylnitrosourea the phosphates residues located in three regions of tRNA Ser : at the variable arm (phosphates 46-47c, 47o, 47p), the T stem-loop (P50, P53, P54) and the acceptor stem (P67-P69) [30] (Fig. 3).…”
supporting
confidence: 90%
See 1 more Smart Citation
“…Furthermore, this recognition is based on the shape rather than on the specific nucleotide sequence, which fits well with the biochemical data [26,27]. These data are also in good agreement with those obtained by us in the solution, where SerRS TT protected from alkylation by ethylnitrosourea the phosphates residues located in three regions of tRNA Ser : at the variable arm (phosphates 46-47c, 47o, 47p), the T stem-loop (P50, P53, P54) and the acceptor stem (P67-P69) [30] (Fig. 3).…”
supporting
confidence: 90%
“…Co-crystal structures of Ser RS, LeuRS, and TyrRS that aminoacylate the type 2 tRNAs together with the footprinting and biochemical data show that the enzymes recognize the unique core domain shape arising from the large stem-loop variable region. The structural description of three bacterial tRNAs with the long variable arms, tRNA Ser , tRNA Leu and tRNA Tyr , has provided an explanation of how the systematic differences between them (correlate insertions in the D loop and the base of the long variable arm) lead to the unique core structure and long-variable-arm orientation in each case [18,30,45,51,60,62]. The recognition by SerRS, LeuRS and TyRS of distinct globular shape in these type 2 tRNAs as a mechanism for selectivity is related to so-called «indirect readout», because usually most or all of the interactions are made with the sugar-phosphate backbone [45].…”
mentioning
confidence: 99%