| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-108 |
Sentence |
denotes |
Identification and characterization of a novel cAMP receptor protein in the cyanobacterium Synechocystis sp. |
| T2 |
109-118 |
Sentence |
denotes |
PCC 6803. |
| T3 |
119-165 |
Sentence |
denotes |
Three open reading frames of Synechocystis sp. |
| T4 |
166-282 |
Sentence |
denotes |
PCC 6803 encoding a domain homologous with the cAMP binding domain of bacterial cAMP receptor protein were analyzed. |
| T5 |
283-563 |
Sentence |
denotes |
These three open reading frames, sll1371, sll1924, and slr0593, which were named sycrp1, sycrp2, and sypk, respectively, were expressed in Escherichia coli as His-tagged or glutathione S-transferase fusion proteins and purified, and their biochemical properties were investigated. |
| T6 |
564-740 |
Sentence |
denotes |
The results obtained for equilibrium dialysis measurements using these recombinant proteins suggest that SYCRP1 and SYPK show a binding affinity for cAMP while SYCRP2 does not. |
| T7 |
741-823 |
Sentence |
denotes |
The dissociation constant of His-tagged SYCRP1 for cAMP is approximately 3 microM. |
| T8 |
824-1037 |
Sentence |
denotes |
A cross-linking experiment using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide revealed that His-tagged SYCRP1 forms a homodimer, and the presence or absence of cAMP does not affect the formation of the homodimer. |
| T9 |
1038-1192 |
Sentence |
denotes |
The amino acid sequence reveals that SYCRP1 has a domain similar to the DNA binding domain of bacterial cAMP receptor protein in the COOH-terminal region. |
| T10 |
1193-1353 |
Sentence |
denotes |
Consistent with this, His-tagged SYCRP1 forms a complex with DNA that contains the consensus sequence for E. coli cAMP receptor protein in the presence of cAMP. |
| T11 |
1354-1430 |
Sentence |
denotes |
These results strongly suggest that SYCRP1 is a novel cAMP receptor protein. |
