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. 1998 May;18(5):2617–2628. doi: 10.1128/mcb.18.5.2617

TABLE 1.

DNA binding affinities of rSSRP1

Oligonucleotide Kd (nM)e DNA binding specificityf Binding site sequenceg
Wild type 2.3 1.0 GATTCTGTTTTAACAGCTTT
−422 mutation >240 <0.010 GATTCTGTTTTAACAGATTT
−425 mutation >100 <0.023 GATTCTGTTTTAAAAGCTTT
Clustered mutationsa >140 <0.016 CATTATCTTTAAAGAACTTT
−435 mutation 12.4 0.185 GATGCTGTTTTAACAGCTTT
−433 mutation 38 0.061 GATTCGGTTTTAACAGCTTT
V-(D)-J signalb 32 0.072 GATCCCACAGTGCTCCAGGGCTGAACAAAAACCGAATT
GATAc >500 <0.005 GGGCAACTGATAAGGATTCC
MAD 7,8d >500 <0.005 GAAACTAAGGTACAGAAGTT
a

This oligonucleotide contains a cluster of six point mutations within PRE II (51). 

b

T160, the murine ortholog of SSRP1, was isolated from a cDNA expression library by using an oligonucleotide containing a murine V-(D)-J RSS (40). 

c

GATA binding site of the mouse α1-globin promoter (52). 

d

An irrelevant DNA sequence upstream of the PRE II DNA recognition element of the ɛ-globin gene (50). 

e

Individual point mutations were characterized previously for PREIIBF binding (15). A subset of these was used to calculate Kds for rSSRP1. 

f

Defined as the ratio of the wild-type Kd to test sequence Kd. 

g

Mutated nucleotides are underlined.