| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.75710218 |
| These results indicate that ( 1 ) the NF Y histone fold dimer can efficiently associate DNA during nucleosome formation ; ( 2 ) it has an intrinsic affinity for H 3 H4 but does not form octamers ; and ( 3 ) the interactions between NF YA , NF YB NF YC , and H 3 H4 or nucleosomes are not mutually exclusive . 0.75710218^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :1.0684568 |
| We show that CBF A and CBF C interact with each other to form a CBF A CBF C complex and that CBF B does not interact with CBF A or CBF C individually but that it associates with the CBF A CBF C complex . 1.0684568^^^ Here we report the isolation of a cDNA coding for rat CBF C , demonstrate that recombinant CBF C is required together with CBF A and CBF B to form a CBF DNA complex , and show that CBF C is present in this protein DNA complex together with the other two subunits . 0.60261097^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.91436284 |
| The second class of mutants identified a segment of CBF A that is necessary for interactions between the CBF A / CBF C heterodimer and CBF B to form a CBF heterotrimer . 0.91436284^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.71393098 |
| Two separate domains were identified in the conserved segment of CBF C for interaction with CBF B ; these were located on each side of the CBF A interaction domain . 0.71393098^^^ Biol . 16 : 328 337 , 1996 ) , this study demonstrates that the histone fold motifs of CBF A and CBF C interact with each other to form the CBF A CBF C heterodimer and generate a hybrid surface which then interacts with CBF B to form the heterotrimeric CBF molecule . . 0.70842172^^^ In this study using cross linking and immunoprecipitation methods , we first established that CBF B interacts simultaneously with both subunits of the CBF A CBF C heterodimer to form a heterotrimeric CBF molecule . 0.67789335^^^ Determination of functional domains in the C subunit of the CCAAT binding factor ( CBF ) necessary for formation of a CBF DNA complex : CBF B interacts simultaneously with both the CBF A and CBF C subunits to form a heterotrimeric CBF molecule . 0.56324398^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :1.0312308 |
| The histone fold motifs of CBF A and CBF C interact with each other to form a heterodimer that associates with CBF B to form a heterotrimeric CBF molecule , which then binds to DNA . . 1.0312308^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.6558046 |
| The nature of the association of CBF B with CBF A / CBF C was also revealed by studying the inhibition of CBF DNA complex formation by the mutant CBF B . 0.6558046^^^ Altogether , these results indicated that the specific DNA contact surface of each CBF subunit is generated as a result of interaction between CBF B and CBF A / CBF C heterodimer and that the three CBF subunits interact interdependently with DNA to form a CBF DNA complex . 0.65248053^^^ This study indicated that the association between CBF B and CBF A / CBF C is stabilized upon interaction with DNA , a process likely to favor formation of a high affinity CBF DNA complex . . 0.54990068^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The subunit association and DNA binding properties of the NF Y complex were examined as a function of redox state using recombinant NF YA , NF YB , and NF YC subunits . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NF Y is composed of three subunits , NF YA , NF YB and NF YC , all necessary for DNA binding . ^^^ Sedimentation velocity centrifugation experiments confirm that two pools of NF YB , and most likely NF YC , exist : one associated with NF YA and binding to the CCAAT box ; another involved in high molecular weight complexes . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| We expressed and purified the yeast homology domain of NF YC in bacteria and performed EMSA together with the corresponding conserved domains of NF YA and NF YB , obtaining a CCAAT binding mini NF Y . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The mammalian transcription factor , NF Y ( CBF ) , contains three known subunit components , NF YA ( CBF B ) , NF YB ( CBF A ) , and NF YC ( CBF C ) , which are all required to reconstitute specific CCAAT box DNA binding activity . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The assembled NF YA : B : C complex , and the NF YB : YC , NF YB : YC ( DNA binding subunit interaction domain ) , and NF YC : YB ( DNA binding subunit interaction domain ) heterodimers were sufficient to support stable interaction with human GCN 5 in vitro , suggesting that these histone acetyltransferases interact with a unique surface in the ancient YB : YC histone fold motif . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| We clone Xenopus NF YA , NF YB and NF YC and establish that NF Y is the predominant Y box binding protein in Xenopus oocyte nuclei . ^^^ |
|
| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| It is a trimer formed by NF YA and two putative histone like subunits , NF YB and NF YC , showing similarity to histones H2B and H2A , respectively . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NF YA and NF YC Q rich domains significantly influence bending angles quantitatively , but not qualitatively , since they do not modify DNA orientation . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| Our analysis indicates that ( 1 ) subunit interactions are normal ; ( 2 ) NF YB NF YC and NC2alpha / beta do not form heterodimers and NC 2 can not associate NF YA . ( 3 ) None of the NF Y swaps can complex with TBP on a TATA box . ( 4 ) Specific residues , R 47 and K 49 in NF YC and N 61 in NF YB , are crucial for CCAAT binding . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The mRNA and protein levels of the histone fold containing NF YB and NF YC were invariant , whereas the NF YA protein , but not its mRNA , was maximal in mid S and decreased in G2 / M . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NF Y is a trimeric CCAAT binding factor with histone fold subunits ( NF YB / NF YC ) and bipartite activation domains located on NF YA and NF YC . ^^^ Combinations of mutants indicate that the Q rich domains of NF YA and NF YC are redundant in the trimeric complex . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| Using a mammalian two hybrid system in HeLa cells , it was shown that both Sp 1 and Sp 3 interacted with NF YA but not NF YB and NF YC . ^^^ A subunit interaction domain of NF YA , which forms a heterotrimer with NF YB and NF YC , is not required for these interactions with Sp 1 or Sp 3 . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The 10 element binds RFX ( RFX5 / RFXANK RFXB / RFXAP ) and CREB , while Y binds NF Y / CBF ( NF YA , NF YB , and NF YC ) . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| OsNF YB 1 is capable of heterodimerizing with NF YC , but not trimerizing with NF YA , thus precluding CCAAT binding . ^^^ |
|
| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The six alternatively spliced NF YA isoforms all showed significantly less synergistic transactivation of the CBS 1b promoter with Sp 1 than wild type NF YA , as determined by cotransfections in Drosophila SL 2 cells with NF YB and NF YC . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NF Y is composed of three subunits , NF YA , NF YB , and NF YC , all required for DNA binding . ^^^ |
|
| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NF Y is a ubiquitous CCAAT binding factor composed of NF YA , NF YB and NF YC . ^^^ Some NF YB and NF YC duplicates showed significant evidence of asymmetric evolution but not the NF YA duplicates . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The transcriptional activator NF Y is a heterotrimeric complex composed of NF YA , NF YB , and NF YC , which specifically binds the CCAAT consensus present in about 30 % of eukaryotic promoters . ^^^ While NF YA is imported by an importin beta mediated pathway , the NF YB / NF YC heterodimer is translocated into the nucleus in an importin 13 dependent manner . ^^^ Importin 13 competes with NF YA for binding to the NF YB / NF YC dimer . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| Our results indicate that a third polypeptide , designated CBF C , forms a tight complex with CBF A . ^^^ Together with CBF A and CBF B , CBF C is required for the DNA binding activity of CBF . . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| CBF consists of three subunits , CBF A , CBF B , and CBF C , all three of which are necessary for DNA binding . ^^^ Nuclear extracts from NIH 3T3 cells were first depleted of CBF and then complemented with recombinant CBF B and a highly purified fraction containing native CBF A and CBF C . ^^^ Recombinant full length CBF B together with CBF A and CBF C activated transcription of several alpha 2 ( 1 ) collagen gene promoter constructs . ^^^ We generated a truncated form of CBF B that was still able to bind DNA in the presence of CBF A and CBF C . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| CBF A , CBF B , and CBF C together form the heterotrimeric mammalian CCAAT binding factor , CBF , which binds to DNA to form a CBF DNA complex . ^^^ Two of the subunits , CBF A and CBF C , were coexpressed and purified as a CBF A / CBF C complex . ^^^ Two CBF deletion mutants , one containing full length CBF A and CBF C and a CBF B lacking the NH 2 terminal residues 1 224 , and the other containing full length CBF A and CBF B and a CBF C lacking the COOH terminal residues 114 309 , also stimulated transcription from these promoters , but the level of activation was reduced to half that obtained with the full length CBF subunits . ^^^ In contrast , a CBF deletion mutant protein containing full length CBF A and deleted forms of both CBF B and CBF C showed very little transcription activation from these promoters . ^^^ The transcriptional activity of the CCAAT binding factor CBF is mediated by two distinct activation domains , one in the CBF B subunit and the other in the CBF C subunit . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| The mammalian CCAAT binding factor CBF ( NFY ) consists of three subunits , CBF A , CBF B , and CBF C . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| Previous studies have shown that CBF contains two transcription activation domains : a glutamine rich , serine threonine rich domain present in the CBF B subunit and a glutamine rich domain in the CBF C subunit . ^^^ In this study , by using a series of deletion mutations of CBF B and CBF C in transcription assay in vitro , we further delineated smaller segments in these domains that were sufficient to support transcriptional activation by CBF . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| We now report the isolation of the genes hapB and hapE , which encode proteins with central regions of high similarity to Hap2p and Hap5p of S . cerevisiae and to the CBF B and CBF C proteins of mammals . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| In this report , we demonstrate that Hap2p , Hap3p , and Hap5p assemble via a one step pathway requiring all three subunits simultaneously , as opposed to the mammalian CCAAT binding factor which has been shown to assemble via a two step pathway with CBF A ( Hap3p homolog ) and CBF C ( Hap5p homolog ) forming a stable dimer before CBF B ( Hap2p homolog ) can interact . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| Furthermore , we demonstrate that purified recombinant HAP 2 , HAP 3 , and HAP 5 are able to reconstitute CCAAT binding activity in mobility shift analysis . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| In yeast a single complex of three proteins , termed HAP 2 , HAP 3 , and HAP 5 , binds to this sequence , and in mammals the three components of the equivalent complex ( called variously NF Y , CBF , or CP 1 ) are also represented by single genes . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| To obtain direct evidence for this , we have cloned the hap 2 , hap 3 and hap 5 genes from H . jecorina . ^^^ A . nidulans deltahap strains were functionally complemented in vitro by the overexpressed H . jecorina HAP 2 , HAP 3 and HAP 5 proteins , and they thus represent subunits of the CCAAT binding complex . ^^^ Furthermore , all three proteins ( HAP 2 , HAP 3 and HAP 5 ) were needed to bind to the CAE in the H . jecorina cbh 2 gene promoter in vitro . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| In particular , NFYA and NFYC bound RFXANK / B in vitro . ^^^ |
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| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13952 and P23511 |
Pubmed |
SVM Score :0.0 |
| NA |
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