Genomic Organization

2014 ◽  
pp. 13-18 ◽  
Author(s):  
Girdhar K. Pandey ◽  
Poonam Kanwar ◽  
Amita Pandey
Keyword(s):  
Genomic Organization

Localization of the Br Polymorphism on a 144 bp Exon of the GPIa Gene and Its Application in Platelet DNA Typing

1994 ◽  
Vol 71 (05) ◽  
pp. 651-654 ◽  
Author(s):  
Rainer Kalb ◽  
Sentot Santoso ◽  
Katja Unkelbach ◽  
Volker Kiefel ◽  
Christian Mueller-Eckhardt
Keyword(s):  
Genomic Organization ◽  
Fragment Length Polymorphism ◽  
Human Platelet ◽  
Dna Typing ◽  
Rflp Analysis ◽  
Serological Typing ◽  
Allele Specific ◽  
Polymerase Chain ◽  
Alloimmune Thrombocytopenia ◽  
Rflp Typing

SummaryAlloimmunization against the human platelet alloantigen system Br (HPA-5) is the second most common cause of neonatal alloimmune thrombocytopenia (NAIT) in Caucasian populations. We have recently shown that a single base polymorphism at position 1648 on platelet mRNA coding for GPIa results in an aminoacid substitution at position 505 on the mature GPIa which is associated with the two serological defined Br phenotypes.Since DNA-typing of platelet alloantigens offers possibilities for useful clinical applications, we designed genomic DNA-based restriction fragment length polymorphism (RFLP) typing for Br alloantigens. To establish this technique we analyzed the genomic organization of GPIa adjacent to the polymorphic base. Using the polymerase chain reaction (PCR) of blood cell DNA we have identified two introns (approximately 1.7 and 1.9 kb) flanking a 144 bp coding sequence of the GPIa gene encompassing the polymorphic base 1648. Based on the in- tron sequence, a PCR primer was constructed to amplify a 274 bp fragment which was used for allele-specific RFLP to determine the Br genotypes. The results of RFLP analysis using Mnll endonuclease obtained from 15 donors (2 Br37*, 2 Br^ and 11 Brb/b) correlate perfectly with serological typing by monoclonal antibody-specific immobilization of platelet antigens (MAIPA) assay.

scholarly journals Structure and Function of Major SARS-CoV-2 and SARS-CoV Proteins

2021 ◽  
Vol 15 ◽  
pp. 117793222110258
Author(s):  
Ritesh Gorkhali ◽  
Prashanna Koirala ◽  
Sadikshya Rijal ◽  
Ashmita Mainali ◽  
Adesh Baral ◽  
...  
Keyword(s):  
Genomic Organization ◽  
Membrane Vesicles ◽  
Structural Proteins ◽  
Host Immune System ◽  
Accessory Proteins ◽  
Nonstructural Proteins ◽  
N Protein ◽  
Small Proteins ◽  
Methylation Mark ◽  
And Function

SARS-CoV-2 virus, the causative agent of COVID-19 pandemic, has a genomic organization consisting of 16 nonstructural proteins (nsps), 4 structural proteins, and 9 accessory proteins. Relative of SARS-CoV-2, SARS-CoV, has genomic organization, which is very similar. In this article, the function and structure of the proteins of SARS-CoV-2 and SARS-CoV are described in great detail. The nsps are expressed as a single or two polyproteins, which are then cleaved into individual proteins using two proteases of the virus, a chymotrypsin-like protease and a papain-like protease. The released proteins serve as centers of virus replication and transcription. Some of these nsps modulate the host’s translation and immune systems, while others help the virus evade the host immune system. Some of the nsps help form replication-transcription complex at double-membrane vesicles. Others, including one RNA-dependent RNA polymerase and one exonuclease, help in the polymerization of newly synthesized RNA of the virus and help minimize the mutation rate by proofreading. After synthesis of the viral RNA, it gets capped. The capping consists of adding GMP and a methylation mark, called cap 0 and additionally adding a methyl group to the terminal ribose called cap1. Capping is accomplished with the help of a helicase, which also helps remove a phosphate, two methyltransferases, and a scaffolding factor. Among the structural proteins, S protein forms the receptor of the virus, which latches on the angiotensin-converting enzyme 2 receptor of the host and N protein binds and protects the genomic RNA of the virus. The accessory proteins found in these viruses are small proteins with immune modulatory roles. Besides functions of these proteins, solved X-ray and cryogenic electron microscopy structures related to the function of the proteins along with comparisons to other coronavirus homologs have been described in the article. Finally, the rate of mutation of SARS-CoV-2 residues of the proteome during the 2020 pandemic has been described. Some proteins are mutated more often than other proteins, but the significance of these mutation rates is not fully understood.

scholarly journals Genomic organization of mouse J kappa recombination signal binding protein (RBP-J kappa) gene.

1992 ◽  
Vol 267 (6) ◽  
pp. 4016-4022
Author(s):  
M Kawaichi ◽  
C Oka ◽  
S Shibayama ◽  
A.E. Koromilas ◽  
N Matsunami ◽  
...  
Keyword(s):  
Genomic Organization ◽  
Binding Protein ◽  
Recombination Signal

The genomic organization of the murine Mlc1 ( Wkl1 , KIAA0027 ) gene

2003 ◽  
Vol 110 (4) ◽  
pp. 333-343 ◽  
Author(s):  
V. Steinke ◽  
J. Meyer ◽  
Y. V. Syagailo ◽  
G. Ortega ◽  
H. Hameister ◽  
...  
Keyword(s):  
Genomic Organization

Genomic organization of the metal-mobilizing bacterium Thiobacillus cuprinus

Gene ◽  
1997 ◽  
Vol 187 (1) ◽  
pp. 99-105 ◽  
Author(s):  
Irma Marı́n ◽  
Ricardo Amils ◽  
José P Abad
Keyword(s):  
Genomic Organization
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