2 edition of dynein heavy chain (DHC) gene family in Tetrahymena thermophila and the targeted knockout of a putative outer arm DHC found in the catalog.
dynein heavy chain (DHC) gene family in Tetrahymena thermophila and the targeted knockout of a putative outer arm DHC
Written in English
|Statement||by Wenjie Xu|
|The Physical Object|
|Pagination||iv, 101 leaves :|
|Number of Pages||101|
Each dynein consists of one to three dynein heavy chains (HCs), which encompass the ATPase activity, complexed to intermediate (IC), light-intermediate (LIC), and light chains (LC). This chapter. dynein heavy ch axonemal (LOC) antibody dynein, axonemal, heavy chain 12 (DNAH12) antibody Show all gene names.
Dyneins: Structure, Biology and Disease, Second Edition, offers a broad view of dyneins mechanics, dysfunction, and disease, providing an overview of dyneins from structure and function, to dysfunction and disease. Since the first edition, enormous strides have been taken in understanding dynein structure, its organization in the axoneme, single molecule motor mechanics, and the consequences. In contrast, wdr extracts almost completely lacked all three outer arm heavy chains, while the IFT dynein heavy chain was present in normal amounts. A wdr tpg double mutant builds ∼7-μm immotile flaccid cilia that completely lack dynein arms. These data indicate that WDR92 is a key assembly factor specifically required for the.
All dynein forms that have been identified biochemically are multisubunit proteins. Each has one to three heavy chains (HCs) of > kDa; these correspond to the number of morphologically identifiable heads and contain the motor domains of the molecule. Axonemal dynein is a microtubule-based molecular motor that drives ciliary/flagellar beating in eukaryotes. In axonemal dynein, the outer-arm dynein (OAD) complex, which comprises three heavy chains (α, β, and γ), produces the main driving force for ciliary/flagellar motility. It has recently been s .
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Cytoplasmic dynein. Cytoplasmic dynein, which has a dynein heavy chain book mass of about megadaltons (MDa), is a dimer of dimers, containing approximately twelve polypeptide subunits: two identical "heavy chains", kDa in mass, which contain the ATPase activity and are thus responsible for generating movement along the microtubule; two 74 kDa intermediate chains which are believed to anchor the InterPro: IPR Dynein Axonemal Light Chain 4 (DNAL4) protein is understood to be part of the axonemal (or ciliary and flagellar) complex of dynein molecules (including dynein heavy and light chains) (GO) and a component of the microtubule-based dynein motor complex .In humans, two known axonemal light chain proteins, DNAL1 and DNAL4, sit at the outer edge of the complex.
Cytoplasmic dynein is the main retrograde motor in all eukaryotic cells. This complex comprises different subunits assembled on a cytoplasmic dynein heavy chain 1 (DYNC1H1) dimer.
Cytoplasmic dynein is particularly important for neurons because it carries essential signals and Cited by: The heavy chain of cytoplasmic dynein 2 was initially identified by molecular studies as a heavy chain closely related to the cytoplasmic dynein 1 heavy chain, yet one whose expression level was unregulated during flagellar synthesis.
Further study showed that the primary function of cytoplasmic dynein 2 is to be the motor for one direction of IFT. The dynein heavy chain is enormous, being approximately amino acid residues in length, more than twice the size of myosin II and more than four times the mass of conventional kinesin.
Unlike myosin and kinesin, the predicted secondary structure of the dynein sequence does not readily divide into a globular head and a tail by: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain.
The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and.
GO_DYNEIN_HEAVY_CHAIN_BINDING: Systematic name: M Brief description: Interacting selectively and non-covalently with a heavy chain of the dynein complex.
[GOC:bf] Full description or abstract: Collection: C5: GO gene sets MF: GO molecular function: Source publication: Exact source: GO Related gene sets External links.
Two heavy chain proteins bind together to form the core of the dynein complex. Combinations of intermediate, light intermediate, and light chains make up the rest of the complex.
The protein produced from the DYNC1H1 gene is a heavy chain. Other subunits are produced from different genes. An Allelic Series of Mutations in the Mouse Cytoplasmic Dynein Heavy Chain Gene, Dync1h1.
Overall Conclusions from the Dync1h1 Mutant Mice. The MMTV-DLCS88A Transgenic Mouse. Using Mouse Genetics to Further Unravel the Role of the Cytoplasmic Dynein Heavy Chain. Conclusion. cytoplasmic dynein 2 has a role in intraﬂagellar transport and is required for cilia and ﬂagella assembly .
The core of the cytoplasmic dynein 1 complex is the heavy chain (DYNC1H1) dimer (Figure 1A). Each heavy chain is enormous – a half-megadalton protein – and, perhaps unsurprisingly, serves multiple purposes.
To. Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and.
Moreover, the axonemal dynein arms are composed of 1–3 heavy chains (– kDa), a variable number of intermediate chains (45– kDa), and one or more light chains (8–28 kDa).
To date, exclusion studies of the DNAH9, DNAI2 (13, ††), and LC8 (††) genes have been reported. FOXJ1, a candidate gene, involved in the regulation. ABSTRACT. Dynein is the large molecular motor that translocates to the (‐) ends of microtubules.
Dynein was first isolated from Tetrahymena cilia four decades ago. The analysis of the primary structure of the dynein heavy chain and the discovery that many organisms express multiple dynein heavy chains have led to two insights.
Dynein is the large molecular motor that translocates to the (-) ends of microtubules. Dynein was first isolated from Tetrahymena cilia four decades ago. The analysis of the primary structure of the dynein heavy chain and the discovery that many organisms express multiple dynein heavy chains.
Dynein heavy chain isoforms and axonemal motility The translocation of dynein along microtubules is the basis for a wide variety of essential cellular movements. Dynein was first discovered in the ciliary axoneme, where it causes the directed sliding between outer doublet microtubules that underlies ciliary.
IPR Dynein heavy chain, domain 2, N-terminal IPR Dynein heavy chain, hydrolytic ATP-binding dynein motor region IPR Dynein heavy chain region D6 P-loop domain. IPR Dynein heavy chain, hydrolytic ATP-binding dynein motor region IPR Dynein heavy chain region D6 P-loop domain IPR EF-Hand 1, calcium-binding site.
DYNEIN HEAVY CHAIN DOMAIN 1; DNHD1 Alternative titles; symbols. COILED-COIL DOMAIN-CONTAINING PROTEIN 35 FLJ HGNC Approved Gene Symbol: DNHD1. Cytogenetic location: 11p Genomic coordinates (GRCh Of the full-length dynein sequences available, DNAH7 was most similar to the Drosophila gene product Dhc36C, sharing % identity and % similarity overall (Fig.4 B).
An analysis of the predicted amino acid sequence demonstrated that DNAH7 shares many of the conserved features of dynein heavy chains. Organisms that have cilia or flagella express over a dozen dynein heavy chain genes.
Of these heavy chain genes, most appear to encode axonemal dyneins, one encodes conventional cytoplasmic dynein (MAP1C or DHC1a), and one, here referred to as DHC1b, encodes an unclassified heavy chain. Previous analysis of sea urchin DHC1b (Gibbons et al.
() Mol. Biol. Cell 5, 57–70) indicated that. Introduction. The microtubule motor called cytoplasmic dynein has roles in diverse cellular processes including meiotic and mitotic spindle assembly and function, neuronal transport, and organelle positioning .Cytoplasmic dynein is composed of a dimer of heavy chains (HCs), along with several accessory chains (ACs: intermediate, light intermediate, and light chains).Dynein heavy chains are involved in microtubule-dependent transport processes.
While cytoplasmic dyneins are involved in chromosome or vesicle movement, axonemal dyneins are essential for motility of cilia and flagella. Here we report the isolation of dynein heavy chain .Coordinated movement of the dynein arms causes the entire axoneme to bend back and forth.
IDAs and ODAs have different combinations of protein components (subunits) that are classified by weight as heavy, intermediate, or light chains.
The DNAH5 gene provides instructions for making heavy chain 5, which is found in ODAs. Other subunits are.