The wheat germ protein synthesis system

Seal, Samarendra N.; Schmidt, A; Marcus, Abraham

doi:10.1016/0076-6879(86)18069-4

Cited by 21 publications

(19 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The deduced protein sequence is shown in Fig. 5 and compared with the protein sequences of eIF3k from human 2 and with deduced protein sequences from C. elegans and D. melanogaster genomes. The A. thaliana sequence is 43, 42, and 45% similar to putative human, C. elegans, and D. melanogaster eIF3k, respectively.…”

Section: Eif3 From Plants Resembles Mammalian Eif3mentioning

confidence: 99%

“…The eIF3 complex isolated from wheat germ contains nine or 10 subunits (2,3,37). The expression patterns of some of the subunits of wheat eIF3 indicated differential regulation and expression during seed development and germination and following heat shock (38).…”

Section: Eukaryotic Initiation Factor 3 (Eif3)mentioning

confidence: 99%

“…The mammalian eIF3 complex composition varies depending upon the method of purification (6, 7, 9 -12); however, the mammalian eIF3 complex appears to contain 11 subunits, p170 (17), p116 (18), p110 (19), p66 (20), p44 (21,22), p48 (23), p47 (20), p40 (20), p36 (19), p35 (21) and p28. 2 The S. cerevisiae eIF3 complex was determined to consist of a core complex of five subunits, Tif32p, Prt1p, Nip1p, Tif35p, and Tif34p (13)(14)(15)24) that correspond to mammalian subunits p170, p116, p110, p44, and p36, respectively (see Table II). There are other proteins associated with the S. cerevisiae eIF3 complex, TIF31p (Clu1p; Ref.…”

Section: Eukaryotic Initiation Factor 3 (Eif3)mentioning

confidence: 99%

“…Mammalian eIF4B, another mRNA-associated initiation factor, was shown also to interact with mammalian eIF3 (36). Interestingly, a similar interaction of S. cerevisiae eIF4B and S. cerevisiae eIF3 could not be demonstrated, suggesting that there may be some fundamental differences in the way eIF3 functions in different organisms (25).The eIF3 complex isolated from wheat germ contains nine or 10 subunits (2,3,37). The expression patterns of some of the subunits of wheat eIF3 indicated differential regulation and expression during seed development and germination and following heat shock (38).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Plant Initiation Factor 3 Subunit Composition Resembles Mammalian Initiation Factor 3 and Has a Novel Subunit

Burks

Bezerra

Le³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Eukaryotic initiation factor 3 (eIF3) is a multisubunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. Recently, the subunits of mammalian and Saccharomyces cerevisiae eIF3 were identified, and substantial differences in the subunit composition of mammalian and S. cerevisiae were observed. Mammalian eIF3 consists of 11 nonidentical subunits, whereas S. cerevisiae eIF3 consists of up to eight nonidentical subunits. Only five of the subunits of mammalian and S. cerevisiae are shared in common, and these five subunits comprise a "core" complex in S. cerevisiae. eIF3 from wheat consists of at least 10 subunits, but their relationship to either the mammalian or S. cerevisiae eIF3 subunits is unknown. Peptide sequences derived from purified wheat eIF3 subunits were used to correlate each subunit with mammalian and/or S. cerevisiae subunits. The peptide sequences were also used to identify Arabidopsis thaliana cDNAs for each of the eIF3 subunits. We report seven new cDNAs for A. thaliana eIF3 subunits. A. thaliana eIF3 was purified and characterized to confirm that the subunit composition and activity of wheat and A. thaliana eIF3 were similar. We report that plant eIF3 closely resembles the subunit composition of mammalian eIF3, having 10 out of 11 subunits in common. Further, we find a novel subunit in the plant eIF3 complex not present in either mammalian or S. cerevisiae eIF3. These results suggest that plant and mammalian eIF3 evolved similarly, whereas S. cerevisiae has diverged. Eukaryotic initiation factor 3 (eIF3)1 is the most complex and least understood of the protein synthesis initiation factors. eIF3 has been purified from wheat germ (1-3), HeLa cells (4, 5), rabbit reticulocytes (6 -12), and Saccharomyces cerevisiae (13)(14)(15)(16). Depending upon the organism and method of purification, there are 6 -11 nonidentical subunits present in functional eIF3 complexes that have been isolated and characterized. Recently, the subunits from the human and S. cerevisiae eIF3 complex have all been identified and sequenced. Surprisingly, there are substantial differences in the subunit composition between mammalian and S. cerevisiae eIF3 complexes. The mammalian eIF3 complex composition varies depending upon the method of purification (6, 7, 9 -12); however, the mammalian eIF3 complex appears to contain 11 subunits, p170 (17), p116 (18), p110 (19), p66 (20), p44 (21, 22), p48 (23), p47 (20), p40 (20), p36 (19), p35 (21) and p28.2 The S. cerevisiae eIF3 complex was determined to consist of a core complex of five subunits, Tif32p, Prt1p, Nip1p, Tif35p,24) that correspond to mammalian subunits p170, p116, p110, p44, and p36, respectively (see Table II). There are other proteins associated with the S. cerevisiae eIF3 complex, TIF31p (Clu1p; Ref. 25), GCD10p (15,26), eI...

show abstract

Section: Eif3 From Plants Resembles Mammalian Eif3mentioning

confidence: 99%

Section: Eukaryotic Initiation Factor 3 (Eif3)mentioning

confidence: 99%

Section: Eukaryotic Initiation Factor 3 (Eif3)mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Plant Initiation Factor 3 Subunit Composition Resembles Mammalian Initiation Factor 3 and Has a Novel Subunit

Burks

Bezerra

Le³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Wheat monosomes were prepared from wheat germ cell-free extracts (Clemens 1984;Seal et al 1986). The extracts were treated with DOC and Triton X-100, final concentration 1% (w/v) each, and layered on a discontinuous sucrose gradient, containing 10 mL of 10% (w/v) sucrose in Buffer A (70 mM KCl, 5 mM MgCl 2 , 20 mM Tris-HCl at pH 7.6, 1 mM DTT) superimposed on 5 mL of 28% (w/v) sucrose in Buffer A.…”

Section: Preparation Of Ribosomesmentioning

confidence: 99%

Secondary structure of two regions in expansion segments ES3 and ES6 with the potential of forming a tertiary interaction in eukaryotic 40S ribosomal subunits

Alkemar

Nygård²

2004

RNA

View full text Add to dashboard Cite

The 18S rRNA of the small eukaryotic ribosomal subunit contains several expansion segments. Electron microscopy data indicate that two of the largest expansion segments are juxtaposed in intact 40S subunits, and data from phylogenetic sequence comparisons indicate that these two expansion segments contain complementary sequences that could form a direct tertiary interaction on the ribosome. We have investigated the secondary structure of the two expansion segments in the region around the putative tertiary interaction. Ribosomes from yeast, wheat, and mouse-three organisms representing separate eukaryotic kingdoms-were isolated, and the structure of ES3 and part of the ES6 region were analyzed using the single-strand-specific chemical reagents CMCT and DMS and the double-strand-specific ribonuclease V1. The modification patterns were analyzed by primer extension and gel electrophoresis on an ABI 377 automated DNA sequencer. The investigated sequences were relatively exposed to chemical and enzymatic modification. This is in line with their indicated location on the surface at the solvent side of the subunit. The complementary ES3 and ES6 sequences were clearly inaccessible to single-strand modification, but available for cleavage by double-strand-specific RNase V1. The results are compatible with a direct helical interaction between bases in ES3 and ES6. Almost identical results were obtained with ribosomes from the three organisms investigated.

show abstract

Knockdown of EIF3D suppresses proliferation of human melanoma cells through G2/M phase arrest

Zhou

Wang

et al. 2015

Biotech and App Biochem

View full text Add to dashboard Cite

Skin cancer is the most common malignancy with increasing incidence rates worldwide. The advanced form of skin cancer, melanoma, is resistant to conventional treatment methods, which motivated researchers to identify an alternative effective therapeutic approach. This study was designed to identify the effects of small interfering RNA (si-RNA) mediated silencing of eukaryotic translation initiation factor 3, subunit D (EIF3D) against melanoma cell survival. Briefly, a lentivirus-mediated RNA interference system was employed to knock down EIF3D expression in A375 and A431 melanoma cells. The cell proliferation was analyzed by methylthiazoletetrazolium (MTT) and colony formation assays. The cell cycle progression was investigated using flow cytometry. Results revealed that si-RNA-mediated knockdown of EIF3D significantly reduced the gene and protein expression levels of EIF3D in melanoma cells. Furthermore, knockdown of EIF3D led to a significant reduction in cell proliferation due to G2 /M phase cell cycle arrest. Apparently, the study demonstrated the critical involvement of EIF3D in the survival and progression of melanoma cells and depletion of EIF3D could be developed as a possible therapeutic option in the gene-targeted treatment of melanoma.

show abstract

The wheat germ protein synthesis system

Cited by 21 publications

References 15 publications

Plant Initiation Factor 3 Subunit Composition Resembles Mammalian Initiation Factor 3 and Has a Novel Subunit

Plant Initiation Factor 3 Subunit Composition Resembles Mammalian Initiation Factor 3 and Has a Novel Subunit

Secondary structure of two regions in expansion segments ES3 and ES6 with the potential of forming a tertiary interaction in eukaryotic 40S ribosomal subunits

Knockdown of EIF3D suppresses proliferation of human melanoma cells through G2/M phase arrest

Contact Info

Product

Resources

About