Copyright © 2016 McGraw-Hill Education. All rights reserved.

Slides:

Advertisements

Similar presentations

FROM DNA TO PROTEIN Transcription – Translation

Advertisements

COLLAGEN CHEMISTRY AND BIOLOGY

I. Introduction Protein Synthesis A. A. History. a. A. Fourcroy – recognized protein as a class of biological molecules b. J. Mulder – Identified proteins.

Collagen Synthesised by VSMC and VEC (perhaps) –soluble procollagen  excreted –cross linked –‘insoluble’ tropocollagen’ –assembled into a fibril (details.

DR AMINA TARIQ BIOCHEMISTRY

New Indications for BMT: Extracellular Matrix Disorder Dystrophic Epidermolysis Bullosa from Jakub Tolar, MD, PhD Blood and Marrow Transplantation University.

Information transferred from DNA to mRNA is translated into an amino acid sequence. 7.3 Translation Information transferred from DNA to mRNA is translated.

DNA Replication When a cell or organism reproduces, a complete set of genetic instructions must pass from one generation to the next.

Express yourself That darn ribosome Mighty Mighty Proteins Mutants RNA to the Rescue

Chapter 17 From Gene to Protein.

Topic 2 Molecular Biology. 2.4 Proteins What do we know about proteins?

Translation The decoding of an mRNA message into a polypeptide chain (aka a protein) is the known as translation The process begins when the mRNA reaches.

RNA and Protein Synthesis Chapter How are proteins made? In molecular terms, genes are coded DNA instructions that control the production of.

FMUC  2009|2010 Turma 7 e 8: Joana Calvão, Joana Laranjinha, Joana Maciel, João Nuno Pereira, Suheila Patel.

FROM DNA TO PROTEIN Transcription – Translation

Space-filling model of the 24-meric cubic core and its constituent trimers. (Left panel) The trimer, where the three catalytic (inner-core) domains (depicted.

Simplified view of the cellular RNA and protein quality surveillance or control systems. Stop-codon introductions as well as splice-site variations, resulting.

Simplified view of the cellular RNA and protein quality surveillance or control systems. Stop-codon introductions as well as splice-site variations, resulting.

Spectrum of different types of human gene mutations logged in Human Gene Mutation Database as of September 13, 1998 ( Source: The.

Reverse-dot ASO analysis for various point mutations causing cystic fibrosis. For each mutation, the PCR product is hybridized to an ASO dot on the left.

Ribosomes and Protein Synthesis

Structure of the A-subunit gene and identified mutations

Epidermolysis bullosa (EB)

Collagen By: Maryam Behmanesh.

Structural organization of the α1(VII) polypeptide of type VII collagen, as deduced by molecular cDNA cloning, and the distribution of COL7A1 mutations.

OCTN2 mRNA in fibroblasts from normal controls and patients with primary carnitine deficiency. PolyA RNA isolated from fibroblasts of normal controls or.

Crystal structure of cdk2, cyclin A-cdk2, and cyclin A-cdk2-p27 complexes. A, The structure of monomeric cdk2. The T-loop is indicated in yellow, and the.

B. A deletion of genomic DNA encompassing only a single exon results in the clinically severe Duchenne muscular dystrophy. A larger deletion encompassing.

Gene-Corrected Fibroblast Therapy for Recessive Dystrophic Epidermolysis Bullosa using a Self-Inactivating COL7A1 Retroviral Vector Joanna Jacków, Matthias.

The Missense Mutation p

Cristina Has, Yinghong He Journal of Investigative Dermatology

Translation 2.7 & 7.3.

Protein Synthesis I. Introduction A. History 1. Protein Structure

Transient Bullous Dermolysis of the Newborn Associated with Compound Heterozygosity for Recessive and Dominant COL7A1 Mutations Nadja Hammami-Hauasli,

Molecular Mechanisms of Junctional Epidermolysis Bullosa: Col15 Domain Mutations Decrease the Thermal Stability of Collagen XVII Laura Väisänen, Cristina.

A Novel COL7A1 Gene Mutation in an Iranian Individual Suffering Dystrophic Epidermolysis Bullosa Hamid Galehdari, Gholamreza Mohammadian, Somayeh Azmoon,

Cellular Metabolism Chapter 4

Progress in Molecular Genetics of Heritable Skin Diseases: The Paradigms of Epidermolysis Bullosa and Pseudoxanthoma Elasticum Jouni Uitto, Leena Pulkkinen,

PLEC1 Mutations Underlie Adult-Onset Dilated Cardiomyopathy in Epidermolysis Bullosa Simplex with Muscular Dystrophy Maria C. Bolling, Hendri H. Pas,

Epidermolysis Bullosa Simplex Associated with Pyloric Atresia Is a Novel Clinical Subtype Caused by Mutations in the Plectin Gene (PLEC1) Hiroyuki Nakamura,

CHAPTER 10 Molecular Biology of the Gene

Novel Homozygous and Compound Heterozygous COL17A1 Mutations Associated with Junctional Epidermolysis Bullosa Michaela Floeth, Heike Schäcke, Nadja Hammami-Hauasli,

Leena Bruckner-Tuderman Molecular Therapy

Eva M. Murauer, Yannick Gache, Iris K

Volume 97, Issue 3, Pages (August 2009)

Unit 7 Part 2 Notes: From Gene to Protein

Arterial complications of vascular Ehlers-Danlos syndrome

A New Case of Keratin 14 Functional Knockout Causes Severe Recessive EBS and Questions the Haploinsufficiency Model of Naegeli–Franceschetti–Jadassohn.

Recurrent COL7A1 Mutations in Japanese Patients with Dystrophic Epidermolysis Bullosa: Positional Effects of Premature Termination Codon Mutations on.

A Homozygous Nonsense Mutation in Type XVII Collagen Gene (COL17A1) Uncovers an Alternatively Spliced mRNA Accounting for an Unusually Mild Form of Non-Herlitz.

Jouni Uitto, Velina S. Atanasova, Qiujie Jiang, Andrew P. South

Long-Range Polymerase Chain Reaction for Specific Full-Length Amplification of the Human Keratin 14 Gene and Novel Keratin 14 Mutations in Epidermolysis.

Normal and Gene-Corrected Dystrophic Epidermolysis Bullosa Fibroblasts Alone Can Produce Type VII Collagen at the Basement Membrane Zone David T. Woodley,

Deletion of the Cytoplasmatic Domain of BP180/Collagen XVII Causes a Phenotype with Predominant Features of Epidermolysis Bullosa Simplex Marcel Huber,

Molecular Therapeutics for Heritable Skin Diseases

Emmanuelle Bitoun, Stéphane Chavanas, Alan D

Extensive growth potential of recessive dystrophic epidermolysis bullosa (RDEB) epidermal keratinocytes Keratinocytes were isolated from the skin of a.

Compound Heterozygosity for a Recessive Glycine Substitution and a Splice Site Mutation in the COL7A1 Gene Causes an Unusually Mild Form of Localized.

Lecture #7 Date _________

Gene-Corrected Fibroblast Therapy for Recessive Dystrophic Epidermolysis Bullosa using a Self-Inactivating COL7A1 Retroviral Vector Joanna Jacków, Matthias.

Genotype–Phenotype Correlation in Recessive Dystrophic Epidermolysis Bullosa: When Missense Doesn't Make Sense Vesarat Wessagowit, Soo-Chan Kim, Se Woong.

The 97 kDa Linear IgA Bullous Dermatosis Antigen is not Expressed in a Patient with Generalized Atrophic Benign Epidermolysis Bullosa with a Novel Homozygous.

Section 13.2 Protein Synthesis.

Segment 5 Molecular Biology Part 1b

Epidermolysis Bullosa: The Expanding Mutation Database

Volume 24, Issue 7, Pages (July 2016)

New Molecular Mechanism for Ullrich Congenital Muscular Dystrophy: A Heterozygous In-Frame Deletion in the COL6A1 Gene Causes a Severe Phenotype Te-Cheng.

2.4 - Proteins.

Presentation transcript:

Copyright © 2016 McGraw-Hill Education. All rights reserved. From: Epidermolysis Bullosa: The Disease of the Cutaneous Basement Membrane Zone GenBank accession numbers for genes of the cutaneous basement membrane zone (BMZ): LAMA3 (X85108, X85107); LAMC2 (U43327, U311787–U31201); LAMB3 (L25541, U17744–U17760); ITGB4 (X51841, U66529–U66541); ITGA6 (X59512; AF166335–AF166343); COL7A1 (L02870, L23982); PLEC1 (Z54367, U53204, U53834, U63609–U63610); BPAG1 (L11690, M69225); BPAG2 (U76564–U76604); KRT5 (U05838–U05849); KRT5 (NM000526). The Online Metabolic and Molecular Bases of Inherited Disease, 2014 Legend: Physiology and pathology of type VII collagen. Synthesis of pro α1(VII) collagen polypeptides and their assembly into anchoring fibrils is depicted at the left side of the figure. The mRNA, ≈9 kb in size, is translated on the ribosomes of cells, such as basal keratinocytes, synthesizing type VII collagen (I). Within the intracellular space (IC) three of these polypeptide chains associate and assemble into a triple-helical type VII collagen molecule, which is then secreted (II and III). In the extracellular space (EC) two triple-helical type VII collagen molecules align into an antiparallel dimer in tail-to-tail orientation with overlapping C-terminal ends (IV). The molecules are processed by proteolytic removal of the NC-2 domains (•), and the association of the dimer is stabilized by disulfide bonding (V). A large number of the dimer molecules laterally assemble in register into anchoring fibrils which contain, at both ends, intact amino-terminal NC1 domains with adhesive properties (VI). In the presence of a mutation in the COL7A1 gene, type VII collagen pathology can manifest as different variants of dystrophic EB. For example, PTCs result in the synthesis of truncated polypeptides unable to form anchoring fibrils, and cause severe Hallopeau-Siemens type of recessive dystrophic EB (HS-RDEB). In the milder, recessively inherited forms of dystrophic EB, known as the Mitis variant (M-RDEB), missense mutations either in a homozygous state or compound heterozygous with a premature termination codon mutation in trans can prevent the assembly of type VII collagen dimers. In case of dominantly inherited dystrophic EB (DDEB), a characteristic mutation is a glycine substitution within the collagenous domain of type VII collagen, which interferes with the packing of the anchoring fibrils and/or compromises the stability of the triple-helical conformation of the type VII collagen molecule. (From Järvikallio et al.36 Used with permission.) Date of download: 9/18/2016 Copyright © 2016 McGraw-Hill Education. All rights reserved.