A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation.
about
The B-box dominates SAP-1-SRF interactions in the structure of the ternary complexc-fos transcriptional activation and repression correlate temporally with the phosphorylation status of TCFDimerization specificity of Arabidopsis MADS domain homeotic proteins APETALA1, APETALA3, PISTILLATA, and AGAMOUSRegulation of the cfos serum response element by C/EBPbetaPhosphorylation-dependent formation of a quaternary complex at the c-fos SREThe Swi5 zinc-finger and Grf10 homeodomain proteins bind DNA cooperatively at the yeast HO promoterTup1p represses Mcm1p transcriptional activation and chromatin remodeling of an a-cell-specific gene.Yeast RLM1 encodes a serum response factor-like protein that may function downstream of the Mpk1 (Slt2) mitogen-activated protein kinase pathway.Mcm1 regulates donor preference controlled by the recombination enhancer in Saccharomyces mating-type switching.Molecular determinants of the cell-cycle regulated Mcm1p-Fkh2p transcription factor complex.The Saccharomyces cerevisiae MADS-box transcription factor Rlm1 is a target for the Mpk1 mitogen-activated protein kinase pathway.DNA-binding specificity of Mcm1: operator mutations that alter DNA-bending and transcriptional activities by a MADS box proteinERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivationMyocyte enhancer factor (MEF) 2C: a tissue-restricted member of the MEF-2 family of transcription factorsTemporal relationship between the transcription of two Arabidopsis MADS box genes and the floral organ identity genes.Functional domains of the floral regulator AGAMOUS: characterization of the DNA binding domain and analysis of dominant negative mutations.Multiple interactions amongst floral homeotic MADS box proteins.The transcription factors Tec1 and Ste12 interact with coregulators Msa1 and Msa2 to activate adhesion and multicellular development.DNA-binding properties of Arabidopsis MADS domain homeotic proteins APETALA1, APETALA3, PISTILLATA and AGAMOUS.Identification of a new hybrid serum response factor and myocyte enhancer factor 2-binding element in MyoD enhancer required for MyoD expression during myogenesisIsolation and characterization of the binding sequences for the product of the Arabidopsis floral homeotic gene AGAMOUS.Activation of the serum response factor by p65/NF-kappaBRas-dependent and -independent pathways target the mitogen-activated protein kinase network in macrophages.MCM1 point mutants deficient in expression of alpha-specific genes: residues important for interaction with alpha 1.MCM1 binds to a transcriptional control element in Ty1Two pathways for serum regulation of the c-fos serum response element require specific sequence elements and a minimal domain of serum response factor.Multiple regulatory elements contribute differentially to muscle creatine kinase enhancer activity in skeletal and cardiac muscle.Functional domains of the yeast STE12 protein, a pheromone-responsive transcriptional activatorIdentification of transcriptional activation and inhibitory domains in serum response factor (SRF) by using GAL4-SRF constructsA Mep2-dependent transcriptional profile links permease function to gene expression during pseudohyphal growth in Saccharomyces cerevisiaeA library of yeast genomic MCM1 binding sites contains genes involved in cell cycle control, cell wall and membrane structure, and metabolismMapping the protein regions responsible for the functional specificities of the Arabidopsis MADS domain organ-identity proteins.DNA binding properties of two Arabidopsis MADS domain proteins: binding consensus and dimer formation.DNA binding specificity determinants in MADS-box transcription factors.Transactivation of the Moloney murine leukemia virus and T-cell receptor beta-chain enhancers by cbf and ets requires intact binding sites for both proteins.Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase Erk2.The transcription factors Elk-1 and serum response factor interact by direct protein-protein contacts mediated by a short region of Elk-1.Identification of amino acids essential for DNA binding and dimerization in p67SRF: implications for a novel DNA-binding motif.Ternary complex formation over the c-fos serum response element: p62TCF exhibits dual component specificity with contacts to DNA and an extended structure in the DNA-binding domain of p67SRF.The yeast alpha 1 and MCM1 proteins bind a single strand of their duplex DNA recognition site
P2860
Q24550909-0637E02F-95A9-4F90-8492-239C71AE2803Q24564617-BB05A1C5-3587-4B4A-8BBB-B1DE9E92762AQ24601528-25A061A9-AD4C-4CDB-A171-5F9FC5C6D284Q24647062-B97B8179-3897-42C4-8614-9E6D5FC6E97DQ24650677-94576840-5383-4D2D-89E7-FE74864C588AQ27931187-B27CD9B5-8C26-4F68-B84A-4489381D0847Q27931501-005C1B84-693B-46B5-A903-80709CBC7641Q27936298-4661A6EC-62FD-48E5-9D2B-3A93635B4A57Q27936567-4D451050-B424-473B-BB9E-B8FBDA3C8164Q27937512-B5C3CBDE-77ED-4FBF-862A-D3201B58DD72Q27939358-20BCE003-1E16-457D-9825-76D879C59EE3Q27940331-0125F01B-148C-491A-8AC0-50550FC5CD46Q28578241-D3A3AB07-303C-489C-B2EC-97D50B6F7A70Q28588872-EA46ED03-004E-4633-846C-69CE1571ADE2Q33366879-2BB234BB-A5BF-43D5-9A19-86C0FC1234F4Q33367686-6727A7A7-B6ED-4DFE-AA4E-6A75D88438A0Q33367826-A6989BA8-EF2E-4840-AA45-25E85499DA8FQ33743589-428B5AE6-7492-40E2-A828-3382CBCE9957Q34608044-BF521413-5A35-41F9-91B8-55D072D396E7Q35810656-1CA7B4DA-8B90-43F5-B085-9D92A03AD5E1Q35859767-24E8CAAF-65F8-425A-B1B1-A52091CCEED6Q35900365-FFDAE1AB-59A2-4A8B-8CA7-33DA5D5AE6A7Q36567137-0BA51F53-9F9B-45AB-98AA-30DCBF7E60F9Q36650349-4234B096-C656-439B-930A-BB8BCFD741BDQ36658284-0AA17860-5BF0-48DE-A90B-E20F05CDE874Q36665209-B44180C3-7D69-4179-99B1-12DBCF7743AEQ36681391-737D1C91-3B35-48F1-A647-1079592112F8Q36687549-53C1F9AD-DF69-4DD5-9881-C3FDF0F77290Q36694137-7E2B8E87-0B69-4185-9873-C451B9F10981Q36739913-1902DB49-8459-47C4-960D-EACAC0F98097Q36758212-F480C85E-26E0-4D22-9BAF-057589797E91Q37628649-184AAD47-3125-4A96-9292-844856F798F0Q38287382-E11365D6-C908-4697-A01C-C4C9AE2907F3Q38293002-45356C31-2BD4-41F3-85C7-6C28CF376B72Q38293060-61A99290-019E-42CD-A8C0-426E22C8778FQ38306691-6FACAE20-6F2B-4F6D-8715-A3F543EBF735Q38308517-315121A0-F059-4FFE-A825-9A37B8FB5364Q38322920-68B83476-38F4-47C1-8ED0-D637E747E690Q38326992-2F853D83-99F4-41AC-BE46-BA65BCCA3F8EQ38327027-369A9977-7CDC-4941-A747-8C4BE3CBF830
P2860
A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
A protein domain conserved bet ...... cts ternary complex formation.
@en
type
label
A protein domain conserved bet ...... cts ternary complex formation.
@en
prefLabel
A protein domain conserved bet ...... cts ternary complex formation.
@en
P2860
P1433
P1476
A protein domain conserved bet ...... ects ternary complex formation
@en
P2093
Mueller CG
Nordheim A
P2860
P304
P356
10.1002/J.1460-2075.1991.TB05000.X
P407
P577
1991-12-01T00:00:00Z