| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-143 |
Sentence |
denotes |
A mode of assembly of P0, P1, and P2 proteins at the GTPase-associated center in animal ribosome: in vitro analyses with P0 truncation mutants. |
| T2 |
144-308 |
Sentence |
denotes |
Ribosomal P0, P1, and P2 proteins, together with the conserved domain of 28 S rRNA, constitute a major part of the GTPase-associated center in eukaryotic ribosomes. |
| T3 |
309-406 |
Sentence |
denotes |
We investigated the mode of assembly in vitro by using various truncation mutants of silkworm P0. |
| T4 |
407-643 |
Sentence |
denotes |
When compared with wild type (WT)-P0, the C-terminal truncation mutants CDelta65 and CDelta81 showed markedly reduced binding ability to P1 and P2, which was offset by the addition of an rRNA fragment covering the P0.P1-P2 binding site. |
| T5 |
644-735 |
Sentence |
denotes |
The mutant CDelta107 lost the P1/P2 binding activity, whereas it retained the rRNA binding. |
| T6 |
736-952 |
Sentence |
denotes |
In contrast, the N-terminal truncation mutants NDelta21-NDelta92 completely lost the rRNA binding, although they retained P1/P2 binding capability, implying an essential role of the N terminus of P0 for rRNA binding. |
| T7 |
953-1129 |
Sentence |
denotes |
The P0 mutants NDelta6, NDelta14, and CDelta18-CDelta81, together with P1/P2 and eL12, bound to the Escherichia coli core 50 S subunits deficient in L10.L7/L12 complex and L11. |
| T8 |
1130-1342 |
Sentence |
denotes |
Analysis of incorporation of (32)P-labeled P1/P2 into the 50 S subunits with WT-P0 and CDelta81 by sedimentation analysis indicated that WT-P0 bound two copies of P1 and P2, but CDelta81 bound only one copy each. |
| T9 |
1343-1509 |
Sentence |
denotes |
The hybrid ribosome with CDelta81 that appears to contain one P1-P2 heterodimer retained lower but considerable activities dependent on eukaryotic elongation factors. |
| T10 |
1510-1620 |
Sentence |
denotes |
These results suggested that two P1-P2 dimers bind to close but separate regions on the C-terminal half of P0. |
| T11 |
1621-1821 |
Sentence |
denotes |
The results were further confirmed by binding experiments using chimeric P0 mutants in which the C-terminal 81 or 107 amino acids were replaced with the homologous sequences of the archaebacterial P0. |
