protein splicing

タンパク質スプライシング

WordNet

any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/07/06 08:27:48」(JST)

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Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment (called an intein) is removed from a precursor protein with a ligation of C-terminal and N-terminal external proteins (called exteins) on both sides. The splicing junction of the precursor protein is mainly a cysteine or a serine, which are amino acids containing a nucleophilic side chain. The protein splicing reactions which are known now do not require exogenous cofactors or energy sources such as adenosine triphosphate (ATP) or guanosine triphosphate (GTP). Normally, splicing is associated only with pre-mRNA splicing.

Types of inteins

The type of the splicing proteins is categorized into four classes: maxi-intein, mini-intein, trans-splicing intein, and alanine intein. The maxi-inteins are N- and C-terminal splicing domains containing an endonuclease domain. The mini-inteins are typical N- and C-terminal splicing domains; however, the endonuclease domain is not present. The trans-splicing inteins are split inteins which are divided into N-termini and C-termini. Alanine inteins have the splicing junction of an alanine instead of a cysteine or a serine, in both of which the protein splicing occurs.

History

Protein splicing was unanticipated and discovered by two groups (Anraku ^[1] and Stevens ^[2]) in 1990. They both discovered a Saccharomyces cerevisiae VMA1 in a precursor of a vacuolar H⁺-ATPase. The amino acid sequence of the N- and C-termini corresponded to 70% of that of a vacuolar H⁺-ATPase from other organisms, while the amino acid sequence of the central position corresponded to 30% of that of the yeast HO nuclease

References

^ Hirata R, Ohsumk Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y (April 1990). "Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae". J. Biol. Chem. 265 (12): 6726–33. PMID 2139027.
^ Kane PM, Yamashiro CT, Wolczyk DF, Neff N, Goebl M, Stevens TH (November 1990). "Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase". Science 250 (4981): 651–7. doi:10.1126/science.2146742. PMID 2146742.

External links

Short review
Starokadomskyy PL. Protein Splicing, 2007
Protein splicing mechanism and intein structure
Protein Splicing at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

SRPK1 facilitates tumor cell growth via modulating the small nucleolar RNA expression in gastric cancer.

Li Y, Yu S, Wang X, Ye X, He B, Quan M, Gao Y.
Journal of cellular physiology. 2019 Aug;234(8)13582-13591.
Serine-arginine protein kinase 1 (SRPK1) is the main regulator in alternative splicing by phosphorylating splicing factors rich in serine/arginine repeats. Its overexpression has been found in multiple cancer types and contributes to cancer development. Here we report the role of SRPK1 and underlyin
PMID 30633341

Hypoxia alters splicing of the cancer associated Fas gene.

Peciuliene I, Vilys L, Jakubauskiene E, Zaliauskiene L, Kanopka A.
Experimental cell research. 2019 Jul;380(1)29-35.
The removal of introns from mRNA precursors (pre-mRNAs) is an essential step in eukaryotic gene expression. The splicing machinery heavily contributes to biological complexity and especially to the ability of cells to adapt to altered cellular conditions. Hypoxia also plays a key role in the pathoph
PMID 31002816

The miR-317 functions as a negative regulator of Toll immune response and influences Drosophila survival.

Li R, Huang Y, Zhang Q, Zhou H, Jin P, Ma F.
Developmental and comparative immunology. 2019 06;95()19-27.
The miR-317 has been revealed to involve in the reproductive response and the larval ovary morphogenesis of Drosophila. However, whether the miR-317 can also regulate Drosophila innate immune responses, which remains unclear to date. Here we have verified that miR-317 can directly target the 3'UTR o
PMID 30708026

Japanese Journal

Enhancing recombinant protein production in human cell lines with a constitutive transport element and mRNA export proteins.

Aihara Yuki,Fujiwara Naoko,Yamazaki Tomohiro,Kambe Taiho,Nagao Masaya,Hirose Yutaka,Masuda Seiji
Journal of biotechnology 153(3-4), 86-91, 2011-05-20
… Recent research into mRNA maturation processes in the nucleus has identified a number of proteins involved in mRNA transcription, capping, splicing, end processing and export. … Here, we showed that the use of a CTE enhanced the expression of recombinant protein in human cell lines. … The co-expression of reporter proteins and Tap-p15 also enhanced recombinant protein expression. …
NAID 120003072129

Chemical treatment enhances skipping of a mutated exon in the dystrophin gene.

Nishida Atsushi,Kataoka Naoyuki,Takeshima Yasuhiro,Yagi Mariko,Awano Hiroyuki,Ota Mitsunori,Itoh Kyoko,Hagiwara Masatoshi,Matsuo Masafumi
Nature communications 2, 2011-05-10
… 2011-05-11.Duchenne muscular dystrophy (DMD) is a fatal muscle wasting disease caused by a loss of the dystrophin protein. … Control of dystrophin mRNA splicing to convert severe DMD to a milder phenotype is attracting much attention. … Although the mutation generates a stop codon, a small amount of internally deleted, but functional, dystrophin protein is produced in the patient cells. …
NAID 120003001398

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[1] Hirata R, Ohsumk Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y (April 1990). "Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae". J. Biol. Chem. 265 (12): 6726–33. PMID 2139027.

[2] Kane PM, Yamashiro CT, Wolczyk DF, Neff N, Goebl M, Stevens TH (November 1990). "Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase". Science 250 (4981): 651–7. doi:10.1126/science.2146742. PMID 2146742.

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