The RNA codon will be GAU, pairing Cytosine-Thymine-Adenine DNA codon with Guanine-Adenine-Uracil RNA codon. This codon is the Amino Acid, Aspartic Acid. In this codon we see Uracil which is the counterpart of Thymine in the RNA.
Their is no genetic diversity and all of the offspring will be the same and also if one parent has a deadly mutation, all of the offspring will get it.
Answer:
B
Explanation:
It plays an important role in how the body uses carbohydrates and fats. It is also needed for the body to make protein for the growth, maintenance, and repair of cells and tissues. Phosphorus also helps the body make ATP, a molecule the body uses to store energy. Phosphorus works with the B vitamins.
I am guessing an Ecological Relationship as it is dependent on it's environment
Protein-protein interactions within the CARMA1-BCL10-MALT1 complex:
- The T-cell receptor and B-cell receptor-dependent NF-B induction and lymphocyte activation are mediated by the CBM complex, which is made up of the proteins CARMA1, BCL10, and MALT1.
- Each of the proto-oncoproteins CARMA1, BCL10, and MALT1 is a somatic gain-of-function mutation or chromosomal translocation, and dysregulation of CBM signaling is a characteristic of numerous lymphoid malignancies, including Activated B-cell Diffuse Large B-cell Lymphoma.
- Moreover, a number of immunological dysregulation diseases have been linked to both gain- and loss-of-function germline mutations in CBM complex proteins.
- Over the past ten years, careful examination of the interactions of CBM components has yielded a wealth of detailed structural knowledge.
- Here, we discuss important discoveries about the molecular nature of these protein-protein interactions that have helped the research develop a detailed understanding of how these proteins come together to form high-order filamentous CBM complexes.
- Approaches to therapeutic suppression of the CBM complex have thus far centered on obstructing MALT1 protease activity in order to treat lymphoid malignancy and/or autoimmunity.
- The structural effects of MALT1 protease inhibitors on significant protein-protein interactions are also reviewed in detail.
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