A nuclear factor that binds to a conserved sequence motif in transcriptional control elements of immunoglobulin genes

Nature ◽  
1986 ◽  
Vol 319 (6049) ◽  
pp. 154-158 ◽  
Author(s):  
Harinder Singh ◽  
Ranjan Sen ◽  
David Baltimore ◽  
Phillip A. Sharp
Keyword(s):  
Transcriptional Control ◽  
Sequence Motif ◽  
Nuclear Factor ◽  
Immunoglobulin Genes ◽  
Conserved Sequence

Myocyte nuclear factor, a novel winged-helix transcription factor under both developmental and neural regulation in striated myocytes

1994 ◽  
Vol 14 (7) ◽  
pp. 4596-4605
Author(s):  
R Bassel-Duby ◽  
M D Hernandez ◽  
Q Yang ◽  
J M Rochelle ◽  
M F Seldin ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Transcriptional Activation ◽  
Myogenic Differentiation ◽  
Specific Binding ◽  
Motor Nerve ◽  
Sequence Motif ◽  
Nuclear Factor ◽  
Winged Helix ◽  
Amino Terminal ◽  
Myocyte Nuclear Factor

A sequence motif (CCAC box) within an upstream enhancer region of the human myoglobin gene is essential for transcriptional activity in both cardiac and skeletal muscle. A cDNA clone, myocyte nuclear factor (MNF), was isolated from a murine expression library on the basis of sequence-specific binding to the myoglobin CCAC box motif and was found to encode a novel member of the winged-helix or HNF-3/fork head family of transcription factors. Probes based on this sequence identify two mRNA species that are upregulated during myocyte differentiation, and antibodies raised against recombinant MNF identify proteins of approximately 90, 68, and 65 kDa whose expression is regulated following differentiation of myogenic cells in culture. In addition, the 90-kDa form of MNF is phosphorylated and is upregulated in intact muscles subjected to chronic motor nerve stimulation, a potent stimulus to myoglobin gene regulation. Amino acid residues 280 to 389 of MNF demonstrate 35 to 89% sequence identity to the winged-helix domain from other known members of this family, but MNF is otherwise divergent. A proline-rich amino-terminal region (residues 1 to 206) of MNF functions as a transcriptional activation domain. These studies provide the first evidence that members of the winged-helix family of transcription factors have a role in myogenic differentiation and in remodeling processes of adult muscles that occur in response to physiological stimuli.

scholarly journals The Crystal Structure of Shikimate Dehydrogenase (AroE) Reveals a Unique NADPH Binding Mode

2003 ◽  
Vol 185 (14) ◽  
pp. 4144-4151 ◽  
Author(s):  
Sheng Ye ◽  
Frank von Delft ◽  
Alexei Brooun ◽  
Mark W. Knuth ◽  
Ronald V. Swanson ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Binding Pocket ◽  
Binding Mode ◽  
Sequence Motif ◽  
Binary Complex ◽  
Shikimate Dehydrogenase ◽  
Conserved Residues ◽  
Conserved Sequence ◽  
Nicotinamide Mononucleotide ◽  
Reversible Reduction

ABSTRACT Shikimate dehydrogenase catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate. We report the first X-ray structure of shikimate dehydrogenase from Haemophilus influenzae to 2.4-Å resolution and its complex with NADPH to 1.95-Å resolution. The molecule contains two domains, a catalytic domain with a novel open twisted α/β motif and an NADPH binding domain with a typical Rossmann fold. The enzyme contains a unique glycine-rich P-loop with a conserved sequence motif, GAGGXX, that results in NADPH adopting a nonstandard binding mode with the nicotinamide and ribose moieties disordered in the binary complex. A deep pocket with a narrow entrance between the two domains, containing strictly conserved residues primarily contributed by the catalytic domain, is identified as a potential 3-dehydroshikimate binding pocket. The flexibility of the nicotinamide mononucleotide portion of NADPH may be necessary for the substrate 3-dehydroshikimate to enter the pocket and for the release of the product shikimate.

Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily

FEBS Journal ◽  
2010 ◽  
Vol 277 (22) ◽  
pp. 4755-4765 ◽  
Author(s):  
Anne-Sophie Delattre ◽  
Bernard Clantin ◽  
Nathalie Saint ◽  
Camille Locht ◽  
Vincent Villeret ◽  
...  
Keyword(s):  
Sequence Motif ◽  
Functional Importance ◽  
Conserved Sequence

scholarly journals Viral DNA Synthesis Defects in Assembly-Competent Rous Sarcoma Virus CA Mutants

2001 ◽  
Vol 75 (1) ◽  
pp. 242-250 ◽  
Author(s):  
Tina M. Cairns ◽  
Rebecca C. Craven
Keyword(s):  
Dna Synthesis ◽  
Rous Sarcoma Virus ◽  
Virus Assembly ◽  
Virus Infectivity ◽  
Sequence Motif ◽  
Viral Dna ◽  
Conserved Sequence ◽  
Rous Sarcoma ◽  
Core Proteins ◽  
Sarcoma Virus

ABSTRACT The major structural protein of the retroviral core (CA) contains a conserved sequence motif shared with the CA-like proteins of distantly related transposable elements. The function of this major region of homology (MHR) has not been defined, in part due to the baffling array of phenotypes in mutants of several viruses and the yeast TY3. This report describes new mutations in the CA protein of Rous sarcoma virus (RSV) that were designed to test whether these different phenotypes might indicate distinct functional subdomains in the MHR. A comparison of 25 substitutions at 10 positions in the RSV conserved motif argues against this possibility. Most of the replacements destroyed virus infectivity, although either of two lethal phenotypes was obtained depending on the residue introduced. At most of the positions, one or more replacements (generally the more conservative substitutions) caused a severe replication defect without having any obvious effects on virus assembly, budding, Gag-Pol and genome incorporation, or protein processing. The mutant particles exhibited a defect in endogenous viral DNA synthesis and showed increased sensitivity of the core proteins to detergent, indicating that the mutations interfere with the formation and/or activity of the virion core. The distribution of these mutations across the MHR, with no evidence of clustering, suggests that the entire region is important for a critical postbudding function. In contrast, a second class of lethal substitutions (those that destroyed virus assembly and release) consists of alterations that are expected to cause severe effects on protein structure by disruption either of the hydrophobic core of the CA carboxyl-terminal domain or of the hydrogen bond network that stabilizes the domain. We suggest that this duality of phenotypes is consistent with a role for the MHR in the maturation process that links the two parts of the life cycle.

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