The murine interleukin 1β gene: structure and evolution

Telford, John L.; Macchia, Giovanni; Massone, A.; Carinci, Valeria; Palla, Emanuela; Melli, Marialuisa

doi:10.1093/nar/14.24.9955

Cited by 60 publications

(20 citation statements)

References 19 publications

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“…Of the IL-is that have been studied, only the human IL-1,f has had its three-dimensional structure published (28). There are, however, a number of other IL-1 sequences available, including IL-1,3 from man, cow, mouse, and rabbit (1,(35)(36)(37), plus the IL-ia sequences from these same species (2,(38)(39)(40). The results of the alignments are presented in Fig.…”

Section: Resultsmentioning

confidence: 99%

Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.

Priestle

Schär

Grütter

1989

Proc. Natl. Acad. Sci. U.S.A.

154

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The structure of human recombinant interleukin lp 8) has been refined by a restrained least-squares method to a crystallographic R factor of 17.2% to 2.0 A resolution. One-hundred sixty-eight solvent molecules have been located, and isotropic temperature factors for each atom have been refined. The overall structure is composed of 12 ,8-strands that can best be described as forming the four triangular faces of a tetrahedron with hydrogen bonding resembling normal antiparallel fl-sheets only at the vertices. Interleukin 1 (IL-1) is a member of a family of cellular mediators known as cytokines. Two distinct species of IL-1 have been characterized, IL-la and IL-1,3. They are about 23% identical in amino acid sequence (1, 2). Both molecules are expressed as a 31-kDa precursor upon activation of a producer cell. The precursor is processed to give a 17.4-kDa carboxyl fragment, which is the mature IL-1f3 molecule (17.8-kDa carboxyl fragment for IL-la). The IL-la precursor is also active, whereas the precursor of IL-1,8 is inactive (3).Processing of the precursor is not well understood. There is no leader sequence (4), and cleavage is believed to be carried out by serine proteases (5, 6). It has been shown that IL-la and IL-1,i bind to the same IL-i-specific receptor (7 Crystals were grown from buffered ammonium sulfate as described (27). The space group is P43, with a = b = 54.9 A and c = 76.8 A with one molecule per asymmetric unit. The structure was solved to 3.0 A resolution (28) by the multiple isomorphous replacement method with two heavy atom derivatives, p-hydroxymercuribenzoate and UO2(NO3)2 combined with phase improvement using solvent flattening (29).High-resolution diffraction data (to 2.0 A) were collected on the X-11 beamline at the Deutsche Electronen Synchrotron at the European Molecular Biology Laboratory Outstation, Hamburg, Federal Republic of Germany, set to a wavelength of 1.464 A. Five randomly oriented crystals were used. Exposure time was 67-157 sec per film pack, depending upon beam strength. An oscillation angle of 1.50 with no overlap between successive films was used. Diffraction data were collected on Kodak DEFO film with two films per film pack. The films were digitized on an Optronics P-1000 film microdensitometer with a 50-gkm raster and a 3.0 optical density scale. The orientation of the crystals was determined by averaging the results of the autoindexing procedure of Kabsch (30) for the first, the last, and a middle film from any one crystal. Typically, 10 films (15°) of data could be collected from one crystal before radiation damage was deemed too severe as judged by visual inspection of the highresolution data on the films. The MoSCO film processing package as integrated into the CCP4 protein crystallographic program package (Darsbury) was used. The results of film processing are shown in Table 1. Despite the random orientation of the crystals, the oscillation data set was about 90% complete, with most of the missing data being at low resolution due to saturation of the spots...

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Section: Resultsmentioning

confidence: 99%

Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.

Priestle

Schär

Grütter

1989

Proc. Natl. Acad. Sci. U.S.A.

154

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“…Mouse IL-1 ␤ -specific primer sequences were: 5 Ј -CTGCTGGTG-TGTGACGTTCCC-3 Ј (sense) and 5 Ј -AGGAAGACACAGATT-CCATGG-3 Ј (antisense) (20). Mouse IL-6-specific primers were: 5 Ј -CCCAACAGACCTGTCTATACC-3 Ј (sense) and 5 Ј -CAGCTT-ATCTGTTAGGAGAGC-3 Ј (antisense) (21).…”

Section: Introductionunclassified

Studies on the contribution of c-fos/AP-1 to arthritic joint destruction.

Shiozawa¹,

Shimizu²,

Tanaka³

et al. 1997

J. Clin. Invest.

101

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“…The entire genomic sequences for human IL-la (21), human IL-1i (14), and murine IL-13 (53) have been previously reported. Despite significant exon sequence diver-* Corresponding author.…”

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confidence: 99%

The functional importance of a cap site-proximal region of the human prointerleukin 1 beta gene is defined by viral protein trans-activation.

Hunninghake¹,

Monks²,

Geist³

et al. 1992

Mol. Cell. Biol.

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Prointerleukin 11 (IL-11) is a cytokine that mediates a broad range of biological activities. Genomic sequences that regulate IL-1l transcription include both inducible regulatory elements located more than 2,700 bp upstream of the transcriptional start site (cap site) and proximal elements located near the TATA box of this gene. In this study, we focused on the identification and characterization of trans-acting nuclear regulatory proteins that bind to the cap site-proximal region of the human IL-1j gene. We identified a protein, termed NFIL-11A (NFPA), that binds to a highly conserved 12-bp DNA sequence (-49 to -38) located upstream of the TATA box motif in both the human and murine IL-1,B genes. The MI-1ct gene, which lacks a TATA motif, does not possess an NFIA-binding sequence within the promoter region, suggesting that NF13A may selectively regulate IL-113 expression. Using electrophoretic mobility shift assays, we identified several distinct DNAprotein complexes that are expressed in a cell-type-specific manner. In monocytic cell lines, the relative abundance of these complexes varies rapidly following stimulation of the cells with phorbol esters or lipopolysaccharide. UV cross-linking analysis identified two distinct DNA-binding polypeptides that comprise distinct complexes. The functional role of NF3A was assessed in transient transfection assays. These data indicate that NFOA is required for both basal and inducible promoter activity in monocytic cells. Furthermore, the human cytomegalovirus immediate-early 1 gene product requires the presence of NFjSA in order to trans-activate the proximal IL-1" promoter in a monocytic cell line. We propose that NF3A is a factor that mediates either direct or indirect activation by the immediate-early 1 gene product. The proximity of this essential factor to the TATA motif suggests a possible role in transcriptional initiation.

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The murine interleukin 1β gene: structure and evolution

Cited by 60 publications

References 19 publications

Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.

Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.

Studies on the contribution of c-fos/AP-1 to arthritic joint destruction.

The functional importance of a cap site-proximal region of the human prointerleukin 1 beta gene is defined by viral protein trans-activation.

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