Final answer:
Serine phosphorylation can activate or inactivate protein function, whereas lysine acetylation tends to unwind nucleosomes and enable gene expression by opening DNA for transcription.
Step-by-step explanation:
In the context of the methyl-phosphate binary switch, serine phosphorylation typically leads to a conformational change in proteins that may activate or inactivate their function. This change is a result of a phosphate group being added to the serine residue by a kinase. On the other hand, lysine acetylation often involves the addition of an acetyl group to the lysine residue of histone proteins, generally catalyzed by histone acetyltransferases (HAT enzymes). Acetylation of lysines tends to unwind nucleosomes and open up DNA for transcription, facilitating gene expression. Conversely, removal of the acetyl group (de-acetylation) promotes chromatin condensation, thereby silencing gene expression. Both modifications play crucial roles in regulating gene transcription by altering chromatin structure and are essential in cellular responses to various signals and environmental stressors.