The human leucine zipper-containing guanine-nucleotide exchange protein elongation factor-1δ

Sanders, J.P.; Raggiaschi, Roberto; Morales, Julia; Möller, W.

doi:10.1016/0167-4781(93)90097-w

Cited by 45 publications

(27 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The GTP binding protein, EF-1␣, is responsible for the transfer of aminoacyl-tRNA to ribosome with the hydrolysis of GTP. The EF-1␤ and EF-1␦ subunits are responsible for the nucleotide exchange activity, which converts the EF-1␣⅐GDP to the active EF-1␣⅐GTP (22)(23)(24). Both ␤ and ␦ sequences appear unrelated other than the C-terminal domain, which is responsible for the nucleotide exchange activity (25).…”

mentioning

confidence: 99%

Kinectin Anchors the Translation Elongation Factor-1δ to the Endoplasmic Reticulum

Ong

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Kinectin has been proposed to be a membrane anchor for kinesin on intracellular organelles. A kinectin isoform that lacks a major portion of the kinesin-binding domain does not bind kinesin but interacts with another resident of the endoplasmic reticulum, the translation elongation factor-1 delta (EF-1␦). This was shown by yeast two-hybrid analysis and a number of in vitro and in vivo assays. EF-1␦ provides the guanine nucleotide exchange activities on EF-1␣ during elongation step of protein synthesis. The minimal EF-1␦-binding domain on kinectin resides within a conserved region present in all the kinectin isoforms. Overexpression of the kinectin fragments in vivo disrupted the intracellular localization of EF-1␦ proteins. This report provides evidence of an alternative kinectin function as the membrane anchor for EF-1␦ on the endoplasmic reticulum and provides clues to the EF-1 complex assembly and anchorage on the endoplasmic reticulum.

show abstract

mentioning

confidence: 99%

Kinectin Anchors the Translation Elongation Factor-1δ to the Endoplasmic Reticulum

Ong

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Elongation factor-1 delta also possesses a nucleotide-exchange activity and interacts with EF-1 alpha and EF-1 beta/gamma. The N-terminal domain of EF-1 delta contains the six-residue leucine-zipper motif typically seen in transcription factors, the function of which is not known (Sanders et al, 1993).…”

mentioning

confidence: 99%

Clinical significance of elongation factor-1 delta mRNA expression in oesophageal carcinoma

et al. 2004

View full text Add to dashboard Cite

Elongation factor-1 (EF-1) delta is a subunit of EF-1, which is a protein complex that participates in the elongation step of mRNA translation and has recently been considered to correlate with oncogenic transformation. However, there has been no information regarding the clinical significance of EF-1 delta mRNA expression in malignant tumours, including oesophageal carcinoma. Thus, we quantitated the expression of EF-1 delta in malignant and benign oesophageal tissues and associated these levels with clinicopathologic parameters of oesophageal carcinoma. Paired oesophageal tissue samples from cancerous and corresponding noncancerous parts were obtained from 52 patients who underwent curative oesophagectomy. Quantitative analyses of EF-1 delta expression were performed using real-time quantitative reverse transcription -polymerase chain reaction. Elongation factor-1 delta mRNA overexpression in cancerous tissues compared to normal counterparts was observed in 38 of 52 (73%) patients. The mean expression level of EF-1 delta mRNA in cancerous tissues was significantly higher than that in noncancerous tissues (Po0.01). A higher expression of EF-1 delta was significantly correlated with lymph node metastases (Po0.05) and advanced stages (Po0.05). Furthermore, the cause-specific survival of patients with a higher expression of EF-1 delta was significantly poorer than those with a lower expression (5-year cause-specific survival rates; 23 and 54%, respectively, Po0.05). The results of this study indicated that EF-1 delta mRNA expression was significantly higher in cancerous compared to noncancerous oesophageal tissues, and a higher expression of EF-1 delta mRNA was correlated with lymph node metastases, advanced disease stages and poorer prognosis for patients with oesophageal carcinoma.

show abstract

“…1A), as exempliˆed by its 57.0, 52.0, 50.7, 50.4, and 49.6z amino acid identities to the EF-1d amino acid sequences from D. melanogaster, 15) A. salina, 2,12) X. laevis, 9) rabbit, 14) and human, 11) respectively. A sequence alignment shows that the C-terminal regions of the EF-1 b sequences are very similar, with signiˆcant homology starting at residue Lys131, which is followed by a region rich in acidic amino acids (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…1A, B). The C-terminal regions of EF-1 b and EF-1d from D. melanogaster, 15) A. salina, 2,6,12) X. laevis, 9,10) rabbit, 13,14) and human 8,11) share greater than 70z amino acid identity, whereas the N-terminal regions share only about 30z amino acid identity. In addition, the C-terminal halves of silk gland EF-1d (amino acid residues 131-262) and EF-1 b (amino acid residues 91-222) are 72.7z identical (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…4) The cDNAs for EF-1 b, g, and d subunits from a number of diŠerent organisms and tissues have been cloned and sequenced. [5][6][7][8][9][10][11][12][13][14][15][16] We have cloned the cDNAs encoding the B. mori silk gland EF-1a, b, g, and d subunits, which consist of 463, 222, 423, and 262 amino acids, respectively. [17][18][19] The carboxyl (C)-terminal regions of the EF-1 b and EF-1d subunits (amino acid residues 91-222 and 131-262, respectively) are 72.7z identical in amino acid sequence, but the similarity of their amino-terminal regions is minor (¿30z).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Interaction between Elongation Factors 1β and 1γ fromBombyx moriSilk Gland

Kamiie

Yamashita

Taira

et al. 2003

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of four subunits: a (51 kDa), b (26 kDa), g (49 kDa), and d (33 kDa). The EF-1a subunit catalyzes the binding of aminoacyl-tRNA to the ribosome concomitant with the hydrolysis of GTP. The EF-1a-bound GDP is then exchanged for GTP by the EF-1 bgd complex. To facilitate analysis of the roles of the individual EF-1 b, g, and d subunits in GDP W GTP exchange on EF-1a, we cloned the cDNAs for these subunits and expressed them in Escherichia coli. EF-1 b, EF-1g, and the carboxyl-terminal half of EF-1d were expressed, puriˆed, and examined for protein:protein interactions by gelˆltration chromatography and by a quartz-crystal microbalance method. An 80-kDa species containing EF-1 b and g subunits in a 1:1 molar ratio was detected by gelˆltration. A higher molecular weight species containing an excess of EF-1g relative to EF-1 b was also detected. The amino-terminal region of EF-1 b (amino acid residues 1-129) was su‹cient for binding to EF-1g. The carboxyl-terminal half of EF-1d did not appear to form a complex with EF-1g.

show abstract

The human leucine zipper-containing guanine-nucleotide exchange protein elongation factor-1δ

Cited by 45 publications

References 10 publications

Kinectin Anchors the Translation Elongation Factor-1δ to the Endoplasmic Reticulum

Kinectin Anchors the Translation Elongation Factor-1δ to the Endoplasmic Reticulum

Clinical significance of elongation factor-1 delta mRNA expression in oesophageal carcinoma

Interaction between Elongation Factors 1β and 1γ fromBombyx moriSilk Gland

Contact Info

Product

Resources

About