Eukaryotic initiation factor 3

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Structure of rabbit eIF3 in the context of the 43S PIC, showing subunits a, c, e, f, h, k, l, and m. Structure of mammalian eIF3 in the context of the 43S preinitiation complex PDB 5A5T.jpg
Structure of rabbit eIF3 in the context of the 43S PIC, showing subunits a, c, e, f, h, k, l, and m.

Eukaryotic initiation factor 3 (eIF3) is a multiprotein complex that functions during the initiation phase of eukaryotic translation. [2] It is essential for most forms of cap-dependent and cap-independent translation initiation. In humans, eIF3 consists of 13 nonidentical subunits (eIF3a-m) with a combined molecular weight of ~800 kDa, making it the largest translation initiation factor. [3] The eIF3 complex is broadly conserved across eukaryotes, but the conservation of individual subunits varies across organisms. For instance, while most mammalian eIF3 complexes are composed of 13 subunits, budding yeast's eIF3 has only six subunits (eIF3a, b, c, g, i, j). [4]

Contents

Function

eIF3 stimulates nearly all steps of translation initiation. [4] eIF3 also appears to participate in other phases of translation, such as recycling, where it promotes the splitting of post-termination ribosomes. [5] In specialized cases of reinitiation following uORFs, eIF3 may remain bound to the ribosome through elongation and termination to promote subsequent initiation events. [6] Research has also indicated that eIF3 plays a role in programmed stop codon readthrough in yeast, by interacting with pre-termination complexes and interfering with decoding. [7]

Interactions

eIF3 binds the small ribosomal subunit (40S) at and near its solvent side and serves as a scaffold for several other initiation factors, the auxiliary factor DHX29, and mRNA. eIF3 is a component of the multifactor complex (MFC) and 43S and 48S preinitiation complexes (PICs). [4] The interactions of eIF3 with other initiation factors can vary amongst species; for example, mammalian eIF3 directly interacts with the eIF4F complex (via eIF4G), while budding yeast lacks this connection. [4] However, both mammalian and yeast eIF3 independently bind eIF1, eIF4B, and eIF5. [2] [8]

Several subunits of eIF3 contain RNA recognition motifs (RRMs) and other RNA binding domains to form a multisubunit RNA binding interface through which eIF3 interacts with cellular and viral IRES mRNA, including the HCV IRES. [4] eIF3 has also been shown to specifically bind m6A modified RNA within 5'UTRs to promote cap-independent translation. [9]

All five core subunits of budding yeast's eIF3 are present in heat-induced stress granules, along with several other translation factors. [10]

Structure

A functional eIF3 complex can be purified from native sources, or reconstituted from recombinantly expressed subunits. [11] [12] Individual subunits have been structurally characterized by X-ray crystallography and NMR, while complexes have been characterized by Cryo-EM. [13] [14] [15] No structure of complete human eIF3 is available, but the nearly-full complex has been determined at medium resolution in the context of the 43S PIC. [1] The structural core of mammalian eIF3 is often described as a five-lobed particle with anthropomorphic features, composed largely of the PCI/MPN octamer. [12] The PCI domains are named for structural similarities between the proteasome cap (P), the COP9 signalosome (C), and eIF3 (I), while the MPN domains are named for structural similarity to the Mpr1-PadI N-terminal domains. [12]

Signaling

eIF3 serves as a hub for cellular signaling through S6K1 and mTOR/Raptor. [16] In particular, eIF3 is bound by S6K1 in its inactive state, and activated mTOR/Raptor binds to eIF3 and phosphorylates S6K1 to promote its release from eIF3. Phosphorylated S6K1 is then free to phosphorylate a number of its own targets, including eIF4B, thus serving as a mechanism of translational control.

Disease

Individual subunits of eIF3 are overexpressed (a, b, c, h, i, and m) and underexpressed (e, f) in multiple human cancers. [3] In breast cancer and malignant prostate cancer, eIF3h is overexpressed. [17] eIF3 has also been shown to bind a specific set of cell proliferation mRNAs and regulate their translation. [18] eIF3 also functions in the life cycles of a number of important human pathogens, including HIV and HCV. In particular, the d-subunit of eIF3 is a substrate of HIV protease, and genetic knockdown of eIF3 subunits d, e, or f results in increased viral infectivity for unknown reasons. [19]

Subunits

The eIF3 subunits exist at equal stoichiometry within the complex, with the exception of eIF3J, which is loosely bound and non-essential for viability in several species. [11] [20] [21] The subunits were originally organized alphabetically by molecular weight in mammals (A as the highest), but the arrangement of molecular weight can vary between species. [22]

SubunitMW (kDa) [A] Key Features
A 167Upregulated in several human cancers. [3] Crosslinks directly to cellular mRNA. [18] Contains PCI domain. [12]
B 92Upregulated in several cancers. [3] Crosslinks directly to cellular mRNA. [18] Contains RRM. [11]
C 105Upregulated in several cancers. [3] Contains PCI domain. [12] Has a human paralog eIF3CL.
D 64Dispensable for growth in fission yeast. [4] Crosslinks directly to cellular mRNA [18] and binds the 5'cap of select mRNAs. [23] Substrate of HIV protease. [19]
E 52Downregulated in breast and lung cancers. [3] Nonessential for growth in fission yeast [24] and Neurospora crassa . [21] Contains PCI domain. [12]
F 38Downregulated in several cancers. [3] Contains MPN domain. [12]
G 36Contains RRM. [11] Crosslinks directly to cellular mRNA. [18]
H 40Upregulated in several cancers. [3] Nonessential for growth in fission yeast, [25] Neurospora crassa, [21] and human cell lines. [26] [27] Contains MPN domain. [12]
I 36Upregulated in several cancers. [3]
J 29Loosely bound, non-stoichiometric subunit. [4] Binds the 40S ribosomal subunit within the decoding center. [28] Nonessential for growth in budding yeast. [4]
K 25Nonessential for growth in Neurospora crassa. [21] Contains PCI domain. [12]
L 67Nonessential for growth in Neurospora crassa. [21] Contains PCI domain. [12]
M 43Upregulated in human colon cancer. [3]

A Molecular weight of human subunits from Uniprot.

See also

Related Research Articles

Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping.

Initiation factors are proteins that bind to the small subunit of the ribosome during the initiation of translation, a part of protein biosynthesis.

Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Several initiation factors form a complex with the small 40S ribosomal subunit and Met-tRNAiMet called the 43S preinitiation complex. Additional factors of the eIF4F complex recruit the 43S PIC to the five-prime cap structure of the mRNA, from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNAiMet promotes gated phosphate and eIF1 release to form the 48S preinitiation complex, followed by large 60S ribosomal subunit recruitment to form the 80S ribosome. There exist many more eukaryotic initiation factors than prokaryotic initiation factors, reflecting the greater biological complexity of eukaryotic translation. There are at least twelve eukaryotic initiation factors, composed of many more polypeptides, and these are described below.

<span class="mw-page-title-main">EIF6</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 6 (EIF6), also known as Integrin beta 4 binding protein (ITGB4BP), is a human gene.

<span class="mw-page-title-main">EIF3I</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit I (eIF3i) is a protein that in humans is encoded by the EIF3I gene.

<span class="mw-page-title-main">EIF3B</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit B (eIF3b) is a protein that in humans is encoded by the EIF3B gene.

<span class="mw-page-title-main">EIF2A</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 2A (eIF2A) is a protein that in humans is encoded by the EIF2A gene. The eIF2A protein is not to be confused with eIF2α, a subunit of the heterotrimeric eIF2 complex. Instead, eIF2A functions by a separate mechanism in eukaryotic translation.

<span class="mw-page-title-main">EIF1AX</span> Protein-coding gene in humans

Eukaryotic translation initiation factor 1A, X-chromosomal (eIF1A) is a protein that in humans is encoded by the EIF1AX gene. This gene encodes an essential eukaryotic translation initiation factor. The protein is a component of the 43S pre-initiation complex (PIC), which mediates the recruitment of the small 40S ribosomal subunit to the 5' cap of messenger RNAs.

<span class="mw-page-title-main">EIF3D</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit D (eIF3d) is a protein that in humans is encoded by the EIF3D gene.

<span class="mw-page-title-main">EIF3J</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit J (eIF3j) is a protein that in humans is encoded by the EIF3J gene.

<span class="mw-page-title-main">EIF1</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 1 (eIF1) is a protein that in humans is encoded by the EIF1 gene. It is related to yeast SUI1.

<span class="mw-page-title-main">EIF3K</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit K (eIF3k) is a protein that in humans is encoded by the EIF3K gene.

The eukaryotic small ribosomal subunit (40S) is the smaller subunit of the eukaryotic 80S ribosomes, with the other major component being the large ribosomal subunit (60S). The "40S" and "60S" names originate from the convention that ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. It is structurally and functionally related to the 30S subunit of 70S prokaryotic ribosomes. However, the 40S subunit is much larger than the prokaryotic 30S subunit and contains many additional protein segments, as well as rRNA expansion segments.

Eukaryotic translation initiation factor 4 G (eIF4G) is a protein involved in eukaryotic translation initiation and is a component of the eIF4F cap-binding complex. Orthologs of eIF4G have been studied in multiple species, including humans, yeast, and wheat. However, eIF4G is exclusively found in domain Eukarya, and not in domains Bacteria or Archaea, which do not have capped mRNA. As such, eIF4G structure and function may vary between species, although the human EIF4G1 has been the focus of extensive studies.

Eukaryotic Initiation Factor 2 (eIF2) is an eukaryotic initiation factor. It is required for most forms of eukaryotic translation initiation. eIF2 mediates the binding of tRNAiMet to the ribosome in a GTP-dependent manner. eIF2 is a heterotrimer consisting of an alpha, a beta, and a gamma subunit.

The eukaryotic initiation factor-4A (eIF4A) family consists of 3 closely related proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA.

<span class="mw-page-title-main">Eukaryotic ribosome</span> Large and complex molecular machine

Ribosomes are a large and complex molecular machine that catalyzes the synthesis of proteins, referred to as translation. The ribosome selects aminoacylated transfer RNAs (tRNAs) based on the sequence of a protein-encoding messenger RNA (mRNA) and covalently links the amino acids into a polypeptide chain. Ribosomes from all organisms share a highly conserved catalytic center. However, the ribosomes of eukaryotes are much larger than prokaryotic ribosomes and subject to more complex regulation and biogenesis pathways. Eukaryotic ribosomes are also known as 80S ribosomes, referring to their sedimentation coefficients in Svedberg units, because they sediment faster than the prokaryotic (70S) ribosomes. Eukaryotic ribosomes have two unequal subunits, designated small subunit (40S) and large subunit (60S) according to their sedimentation coefficients. Both subunits contain dozens of ribosomal proteins arranged on a scaffold composed of ribosomal RNA (rRNA). The small subunit monitors the complementarity between tRNA anticodon and mRNA, while the large subunit catalyzes peptide bond formation.

<span class="mw-page-title-main">Eukaryotic initiation factor 4F</span> Multiprotein complex used in gene expression

Eukaryotic initiation factor 4F (eIF4F) is a heterotrimeric protein complex that binds the 5' cap of messenger RNAs (mRNAs) to promote eukaryotic translation initiation. The eIF4F complex is composed of three non-identical subunits: the DEAD-box RNA helicase eIF4A, the cap-binding protein eIF4E, and the large "scaffold" protein eIF4G. The mammalian eIF4F complex was first described in 1983, and has been a major area of study into the molecular mechanisms of cap-dependent translation initiation ever since.

The 43S preinitiation complex is a ribonucleoprotein complex that exists during an early step of eukaryotic translation initiation. The 43S PIC contains the small ribosomal subunit (40S) bound by the initiation factors eIF1, eIF1A, eIF3, and the eIF2-Met-tRNAiMet-GTP ternary complex (eIF2-TC).

<span class="mw-page-title-main">DHX29</span> Protein-coding gene in the species Homo sapiens

DExH-box helicase 29 (DHX29) is a 155 kDa protein that in humans is encoded by the DHX29 gene.

References

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