The disclosure provides novel methods and compositions for gene editing. In particular, the disclosure relates to compositions and methods of making nucleic acid donor templates for highly efficient and precise gene editing.

The disclosure provides novel methods and compositions for gene editing. In particular, the disclosure relates to compositions and methods of making nucleic acid donor templates for highly efficient and precise gene editing.

H-NOX proteins are mutated to exhibit improved or optimal kinetic and thermodynamic properties for blood gas O.sub.2 delivery. The engineered H-NOX proteins comprise mutations that impart altered O.sub.2 or NO ligand-binding relative to the corresponding wild-type H-NOX domain, and are operative as physiologically compatible mammalian blood O.sub.2 gas carriers. The invention also provides pharmaceutical compositions, kits, and methods that use wild-type or mutant H-NOX proteins for the treatment of any condition for which delivery of O.sub.2 is beneficial.

The present invention provides a method for producing artificial protein sequences and artificial nucleic acid sequences for the linker histone variants H1.0 (also known as histone H1°; H1(0); H5; H1δ; RI H1; or H1 histone family, member 0) and H1x (also known as histone H1.10 or H1 histone family, member X). In particular, the artificial protein sequences produced by the method feature engineered α-helical motifs—three structural motifs in the histone H1 that bind to nucleosomal and/or linker DNA in chromatin. These artificial-sequence histone H1 proteins, when they replace or supplement their wild-type counterparts in vivo, confer multicellular individuals significant resistance to senescence and/or age-related health conditions such as age-related cancer.

The invention provides an isolated peptide comprising a lysine 3-hydroxybutyrylation site, a lysine 3-hydroxybutyrylation specific affinity reagent that specifically binds to the peptide, and a method for detecting protein lysine 3-hydroxybutyrylation in a sample using the reagent.

The invention provides an isolated peptide comprising a lactylated lysine and a specific affinity reagent that specifically binds to a lactylated lysine in a peptide. Also provided are a method for detecting a lactylated lysine in a protein or a fragment thereof using the affinity reagent and a method for isolating the affinity reagent.

Provided herein are screening methods that utilize transgenic nematodes exposed to heat shock conditions, such as agents that increase stability of F-actin. The transgenic nematodes used can be in a wild-type background, functionally deleted for OSG-1, or express human ARHGEF10 in an OSG-1 background. Such transgenic nematodes also express a fluorescent protein, such as GFP. Such methods are in some examples high throughput and automated. Also provided are recombinant nematodes and kits that can be used with such methods.

The invention provides an isolated peptide comprising a lysine 3-hydroxybutyrylation site, a lysine 3-hydroxybutyrylation specific affinity reagent that specifically binds to the peptide, and a method for detecting protein lysine 3-hydroxybutyrylation in a sample using the reagent.

A novel class of transporter protein, referred to as SWEET, GLUE or Gl, is disclosed. These transporters provide a novel system for the transportation of sugars across membranes within a cell and between the inside and outside of a cell. Such transporters are useful for understanding and altering the sugar concentration within certain organs of an organism, and within certain organelles within the cell. These transporters are also useful in protecting plants from a pathogen attack.

A recombinant polypeptide is described which comprises at least one PUF RNA-binding domain capable of specifically binding to a cytosine RNA base. The PUF RNA-binding domain of the polypeptide comprises at least one RNA base-binding motif of the general formula X.sub.1X.sub.2X.sub.3X.sub.4X.sub.5X.sub.6X.sub.7X.sub.8X.sub.9X.sub.10X.sub.11 wherein X.sub.1 is selected from the group including glutamine (Q), valine (V), methionine (M), proline (P), glutamic acid (E), and lysine (K); X.sub.2 is selected from the group including histidine (H), phenylalanine (F), tyrosine (Y), and asparagine (N); X.sub.3 is selected from the group including glycine (G) and alanine (A); X.sub.4 is selected from the group including glycine (G), alanine (A), serine (S), threonine (T) and cysteine (C); X.sub.5 is selected from the group including arginine (R), tyrosine (Y), histidine (H), and asparagine (N); X.sub.6 is selected from the group including phenylalanine (F), leucine (L), and valine (V); X.sub.7 is selected from the group including isoleucine (I), leucine (L), and valine (V); X.sub.8 is arginine (R); X.sub.9 is selected from the group including leucine (L), lysine (K), arginine (R), glutamine (Q), and histidine (H); X.sub.10 is selected from the group including lysine (K), phenylalanine (F), alanine (A), cysteine (C), isoleucine (I), valine (V), leucine (L), and methionine (M); and X.sub.11 is selected from the group including leucine (L), phenylalanine (F), isoleucine (I), and valine (V); and wherein the RNA base-binding motif is operably capable of specifically binding to a cytosine RNA base.