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. 2002 May;76(10):4928–4939. doi: 10.1128/JVI.76.10.4928-4939.2002

TABLE 2.

Dimerization and DNA-binding characteristics of v-Rel mutants

Protein Classa Dimerizationb with:
DNA bindingc with:
v-Reld c-Rel NF-κB1 NF-κB2 RelA v-Reld c-Rel NF-κB1 NF-κB2
v-Rel ++++ ++++ ++++ ++++ ++++ +++ +++ ++++ ++++
M1 I +++ ++++ +++ ++++ +/− ++ +++ +++
M2 II + +++ ++++ + + ++ +
M3 III + ++++ ++++ ++ +
M4 IV + ++ + + +
M5 IV ++++ ++++ + + +
M6 V +++ ++++ ++ +
M7 V +++ ++++ +++ +++
M8 V ++ ++++ + +
M9 V ++++ + +++ +++
a

Each dimerization mutant was assigned to a particular class based on the inability to interact with specific Rel/NF-κB family members.

b

Quantitative liquid β-galactosidase assays were performed to evaluate the formation of homodimers (23.2 ± 1.2) and heterodimers with c-Rel (23.6 ± 1.3), NF-κB1 (135.3 ± 5.1), NF-κB2 (60.7 ± 13.8), and RelA (61.4 ± 1.3). Dimerization: ++++, >75%; +++, 50 to 75%; ++, 25 to 50%; +, <25%; −, none detected. These values represent the β-galactosidase activity relative to that observed for v-Rel.

c

Qualitative assessment of DNA-binding activity relative to v-Rel.

d

Assayed for homodimer formation.