A Protein That Binds to a cis-acting Element of Wheat Histone Genes Has a Leucine Zipper Motif

Tabata, Tetsuya; Takase, Haruhiko; Takayama, Shinobu; Mikami, Koji; Nakatsuka, Atsunori; Kawata, Takefumi; Nakayama, Takuya; Iwabuchi, Masaki

doi:10.1126/science.2772648

Cited by 179 publications

(102 citation statements)

References 25 publications

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“…bZIP910, bZIP911, OBF1, MLIP15 (LIP15), LIP19, At7568 (AT7568) and At1507 (AT1507) form a sub-family more closely related to each other in sequence composition of their bZIP domains than to other bZIP proteins. Other bZIP proteins included are CPRF-1, 2 and 3 (Weisshaar et al, 1991) from parsley; TGA1b (Katagiri et al, 1989) from tobacco, GBF1 (Schindler et al, 1992c) from Arabidopsis, GBF9G, (Meier and Gruissem, 1994) from tomato, HBP1a and HBPlac14 (Mikami et al, 1994;Tabata et al, 1989) from wheat, and OHP1 and O2 (Hartings et al, 1989;Pysh et al, 1993) from maize.…”

Section: Both Bzip Cdnas Contain a Conserved Upstream Open Reading Frmentioning

confidence: 99%

“…Histone genes are expressed in plant tissues which are undergoing cell division. The elements homologous to the bZIP910 and bZIP911 consensus binding motif belong to a hexameric (hex) motif which has been identified functionally as being required for expression from the promoters of a subgroup of histone genes (Mikami et al, 1994;Tabata et al, 1989). These elements are conserved between species and match the extended bZIP911/bZIP910 consensus well.…”

Section: The Tgacgtg Motif Is Present In the Promoters Of Different Gmentioning

confidence: 99%

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Two bZIP proteins from Antirrhinum flowers preferentially bind a hybrid C‐box/G‐box motif and help to define a new sub‐family of bZIP transcription factors

et al. 1998

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SummaryTwo genes encoding bZIP proteins are expressed in flowers of Antirrhinum majus, predominantly in vascular tissues, carpels and anthers. The sequences of cDNA clones encoding these proteins show them to belong to a distinct subfamily of bZIP proteins which also includes LIP19 from rice and MLIPI5 and OBF1 from maize. The sub-family is characterized by the inclusion of very small proteins consisting of essentially a basic domain and a long leucine zipper. Members also have a conserved upstream open reading frame (uORF) in their 5Ј leader sequences, implying a common mode of post-transcriptional control. In vitro, the Antirrhinum bZIP proteins preferentially bind to a novel hybrid C-box/G-box motif which is found in the promoters of some plant histone genes and of some nuclear-encoded genes with plastidial protein products. Expression of the bZIP proteins in transgenic tobacco under control of the CaMV 35S promoter supports the view that they can regulate expression of genes which contain the preferred target motif within their regulatory sequences, although both enhancement and repression of transcript levels of target genes were observed, indicating that the bZIP proteins probably interact with other factors to modulate transcription in different ways, as has been observed for the small MAF family of bZIP proteins in vertebrates.

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Section: Both Bzip Cdnas Contain a Conserved Upstream Open Reading Frmentioning

confidence: 99%

Section: The Tgacgtg Motif Is Present In the Promoters Of Different Gmentioning

confidence: 99%

Two bZIP proteins from Antirrhinum flowers preferentially bind a hybrid C‐box/G‐box motif and help to define a new sub‐family of bZIP transcription factors

et al. 1998

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“…This bipartite structure is characteristic of the bZlP class of DNA binding proteins (Vinson et aL, 1989). To date, 11 cDNAs GBFs have been isolated from five different plant species, all of them are bZlP proteins (Guiltinan et aL, 1990;Meier and Gruissem, 1994;Oeda et aL, 1991;Schindler et aL, 1992a;Tabata et aL, 1989;Weisshaar et al, 1991). Amino acid sequence comparison Maize GBF induced by hypoxia 597 of the plant GBFs shows a high degree of conservation (85% or more identical residues) in the basic domain, the amino acids that are thought to come in contact with the DNA.…”

Section: Structure Of Gbfimentioning

confidence: 99%

Characterization of a maize G‐box binding factor that is induced by hypoxia

Vetten¹,

Ferl²

1995

The Plant Journal

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SummaryG-box cis-acting DNA sequence elements are present in the promoter region of a number of signal-inducible plant genes. In many cases this motif is essential for gene expression. Maize nuclear extracts contain a protein complex that binds specifically to the G-box sequence. Previously, a protein called GF14 was described that is physically associated with the G-box binding complex, but is not a DNA-binding factor in and of itself. This paper reports the isolation of a cDNA encoding a maize G-box binding factor (GBF). The deduced amino acid sequence indicates that maize GBF1 is a basic region-leucine zipper protein. GBF1 binds to the G-box element with specificity similar to that of the binding activity in nuclear extracts. Furthermore, maize GBF1 and the factor detected in nuclear extract are identical in their molecular weight and are immunologicelly related. GBF1 mRNA accumulates rapidly in hypoxicelly induced maize cells prior to the increase in Adhl mRNA levels. Taken together with results that indicate that GBF1 binds to the hypoxia-responsive promoter of maize Adh 1, these observations suggest that GBF1 may be one of the factors involved in the activation of Adh l.

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“…The asparagine (N) and arginine (R) in the consensus sequence are completely conserved in all bZIP proteins described thus far and are shown boxed. Sources for sequences: (02) Schmidt et al (1990); (Fos) Van Straaten et al (1983); (FRAl) Cohen and Curran (1988); (JunB) Ryder et al (1988); (c-Jun) Angel et al (1988); (GCN4) Hinnebusch (1984); (CPCl) Paluh et al (1988); (CREB) Gonzalez et al (1989); (C/EBP) Landschulz et al (1988b); (TGAla) Katagiri et al (1989); (HBPl) Tabata et al (1989). …”

mentioning

confidence: 99%

An arginine to lysine substitution in the bZIP domain of an opaque-2 mutant in maize abolishes specific DNA binding.

Aukerman

Schmidt²,

Burr³

et al. 1991

Genes Dev.

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The opaque-2 {o2) locus in maize encodes a transcription factor involved in the regulation of zein storage proteins. We have shown previously that the 02 protein contains a leucine zipper domain that binds to promoters of 22-kD zein genes. In this paper we characterize an EMS-induced o2 allele, o2-676, that causes a 50% reduction in zein. We have found that the o2-676 mutant protein does not show specific recognition of zein promoter fragments because of the substitution of a lysine residue for an arginine residue within the bZIP domain of o2-676. This particular arginine is conserved within the bZIP domains of all mammalian, fungal, and plant DNA binding proteins of this class. The correlation between this mutation in o2 and the altered pattern of zein expression strongly suggests that 02 regulates transcription of certain members of the zein multigene family through direct interaction with the zein promoters and not through the transcriptional activation of some other regulator of zein gene expression.

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A Protein That Binds to a cis-acting Element of Wheat Histone Genes Has a Leucine Zipper Motif

Cited by 179 publications

References 25 publications

Two bZIP proteins from Antirrhinum flowers preferentially bind a hybrid C‐box/G‐box motif and help to define a new sub‐family of bZIP transcription factors

Two bZIP proteins from Antirrhinum flowers preferentially bind a hybrid C‐box/G‐box motif and help to define a new sub‐family of bZIP transcription factors

Characterization of a maize G‐box binding factor that is induced by hypoxia

An arginine to lysine substitution in the bZIP domain of an opaque-2 mutant in maize abolishes specific DNA binding.

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