The molecular biology of IRBP: application to problems of uveitis, protein chemistry, and evolution.
In closing, molecular biology has helped us in the study of uveitis, in defining the parts of the IRBP molecule that cause EAU/EAP. Simple northern and Southern blotting experiments can answer significant questions in the study of gene structure and expression and in relating these to genetic eye diseases. Molecular biology has provided answers to several long-standing cell biology question such as: where is IRBP synthesized, where is the gene expressed, and how is the IRBP polypeptide processed? In considering how mother nature invented the IRBP gene, the gene structure suggests some interesting alternative models, and causes us to speculate about how large proteins may have evolved. Finally, the determination of the protein sequence helps to put us in the position to ask and answer questions about the function of IRBP. It also allows us to begin to determine the consequences of a nonfunctional IRBP. We don't know the answers to all these questions yet, but the structural analyses and the isolation of these genes and cDNAs, presented here, united with other powerful biological techniques should provide the answers.
Nickerson
J M
JM
LRCMB, NEI, NIH, Bethesda, MD 20892.
Borst
D E
DE
Redmond
T M
TM
Si
J S
JS
Toffenetti
J
J
Chader
G J
GJ
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D005136:Eye Proteins; D006801:Humans; D008969:Molecular Sequence Data; D010870:Pineal Gland / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics; D012160:Retina / Q000378:metabolism; D012177:Retinol-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D014605:Uveitis / Q000209:etiology*; D000099214:Retinol-Binding Proteins, Interstitial
D005136:Eye Proteins; D012333:RNA, Messenger; D012177:Retinol-Binding Proteins; D000099214:Retinol-Binding Proteins, Interstitial