The Signal Sequence Receptor, Alpha (SSRA), also known as SSR1, is a crucial component of the signal sequence receptor complex located in the endoplasmic reticulum (ER) membrane. This receptor plays a significant role in the translocation of proteins across the ER membrane, a process essential for proper protein folding and function.
The SSR complex is composed of two subunits: a 34-kDa glycoprotein encoded by the SSR1 gene and a 22-kDa glycoprotein. The SSR1 gene is known for its complex alternative polyadenylation, resulting in multiple mRNA species and various isoforms . The SSR1 gene is located on chromosome 6 and is highly conserved across different species, indicating its fundamental role in cellular processes.
The primary function of the SSRA is to facilitate the translocation of nascent polypeptides into the ER lumen. This process is critical for the proper folding and post-translational modifications of proteins. The SSRA binds to the signal sequence of the nascent polypeptide, guiding it to the translocon complex in the ER membrane. Once the polypeptide is translocated, the SSRA may also play a role in recycling the translocation apparatus or act as a membrane-bound chaperone to assist in protein folding .
The SSRA is involved in several key cellular processes, including the Unfolded Protein Response (UPR) and cellular responses to stimuli. The UPR is a cellular stress response related to the ER, which is activated in response to the accumulation of unfolded or misfolded proteins in the ER lumen. By facilitating proper protein folding and translocation, the SSRA helps maintain ER homeostasis and prevent cellular stress .
Recombinant SSRA is produced using recombinant DNA technology, which allows for the expression of the SSRA protein in various host systems. This technology is essential for studying the protein’s structure, function, and interactions in a controlled environment. Recombinant SSRA can be used in research to understand its role in protein translocation and its potential implications in disease mechanisms.