1992
DOI: 10.1016/0092-8674(92)90129-z
|View full text |Cite
|
Sign up to set email alerts
|

The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

15
516
2
3

Year Published

1996
1996
2012
2012

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 659 publications
(537 citation statements)
references
References 55 publications
15
516
2
3
Order By: Relevance
“…The DNA binding domain of SRY shares homology with a number of known or suspected transcription factors of the HMG box class [2]. Experiments in vitro suggest that SRY binds linear DNA in a sequence-specific manner [3,4] and causes a bend [5,6]. Mutations in the HMG domain of SRY encoded by XY gonadal dysgenesis patients affect the DNA binding or DNA bending activity of SRY in vitro which is consistent with these activities being necessary for testis development [7].…”
Section: Introductionmentioning
confidence: 59%
See 1 more Smart Citation
“…The DNA binding domain of SRY shares homology with a number of known or suspected transcription factors of the HMG box class [2]. Experiments in vitro suggest that SRY binds linear DNA in a sequence-specific manner [3,4] and causes a bend [5,6]. Mutations in the HMG domain of SRY encoded by XY gonadal dysgenesis patients affect the DNA binding or DNA bending activity of SRY in vitro which is consistent with these activities being necessary for testis development [7].…”
Section: Introductionmentioning
confidence: 59%
“…In the presence of CaM, peptides from two regions of the SRY HMG domain showed an interaction: residues 57-80 (lane 1) and a second, weakly binding region, 131-144, which gave multiple bands (lane 9). No CaM binding was detectable with the other six SRY peptides (lanes [3][4][5][6][7][8]. Binding affinity of SRY peptides 57-80 (QDRVKRPM-NAFIVWSRDQRRKMAL) to CaM was similar to that for the whole HMG box; binding of SRY peptides 131-144 (PRRKAKMLPKNCSL) was about five-fold weaker.…”
Section: Resultsmentioning
confidence: 99%
“…RUNX1 binding to DNA is through its central runt domain, and activation of the class I promoter depends on both its DNA binding and activation domains. LEF1 is an HMG protein whose binding to DNA causes bending of the backbone (34,62,84,85). Neither RUNX1 nor LEF1 alone significantly affected MHC class I expression in the nonlymphocyte HeLa epithelial cell line, which does not express either of these factors (data not shown).…”
Section: Discussionmentioning
confidence: 99%
“…The spatio-temporal expression of genes is controlled by DNA elements called enhancers (Banerji et al 1981) or cis-regulatory modules (CRMs) (Kirchhamer et al 1996). These elements act as docking platforms for transcription factors (TFs), and the combined regulatory cues of all bound TFs results in the activation (or repression) of gene expression (e.g., Stanojevic et al 1991;Giese et al 1992).…”
mentioning
confidence: 99%